Title of Invention: Function of a haptoglobin-haemoglobin receptor and the uses thereof Abstract: The present invention relates to haptoglobin-haemoglobin (Hp-Hb) complex or a part thereof or a mimic thereof being operably linked to a substance and capable of binding a CD163 receptor. Furthermore, the invention relates to a CD163 variant, membrane bound or soluble, capable of binding at least one haptoglobin-haemoglobin (Hp-Hb) complex, and the use of the Hp-Hb complex and the CD163 receptor for therapy. Detailed Description: The present invention relates to haptoglobin-haemoglobin (Hp-Hb) complex or a part thereof or a mimic thereof being operably linked to a substance and capable of binding a CD163 receptor. Furthermore, the invention relates to a CD163 variant, membrane bound or soluble, capable of binding at least one haptoglobin-haemoglobin (Hp-Hb) complex, and the use of the Hp-Hb complex and the CD163 receptor for therapy. BACKGROUND OF THE INVENTION Normal adult haemoglobin consists of a tetramer of four haemoglobin chains, two α-chains and two β-chains. O2 binds to the tetrameric form of haemoglobin and is transported in the blood. Fetal blood comprises fetal haemoglobin, a tetramer consisting of two α-chains and two γ-chains. Further haemoglobin chains have been identified, such as δ-chains, ε-chains, zeta-chains, τ-chains or the S form known to be the mutation seen in haemoglobin of individuals suffering from sickle cell disease. Intravascular lysis of red blood cells (haemolysis) leads to the release of haemoglobin into plasma. This phenomenon occurs during physiological as well as pathological conditions. Pathological complications are severe when accelerated in infectious e.g. malaria), inherited (e.g. side cell anemia), or autoimmune diseases. The haemoglobin tetramers are converted to haemoglobin dimers capable of binding haptoglobin. In the plasma haemoglobin is captured by the acute phase protein haptoglobin. Haptoglobin is a blood plasma protein having a molecular weight of approximately 86,000 to 400,000 and plays an important role in the metabolism of haemoglobin liberated into the blood stream. When liberated excessively in the blood the haemoglobin is excreted into the urine through the renal tubules, resulting in not only an iron loss but also disorders of the renal tubules. Because haptoglobin binds selectively and firmly to haemoglobin in vivo and thereby forms a haemoglobin-haptoglobin complex, it has important functions in the recovery of iron and in the prevention of renal disorders. Hp is synthesised as a single chain, which is post-translationally cleaved into an amino-terminal α chain and a carboxy-terminal β chain. The basic structure of Hp, as found in most mammals, is a homodimer (FIG. 2a), in which the two Hp molecules are linked by a single disulfide bond via their respective ˜9 kDa α chains. In man, a variant with a long α chain is also present in all populations. This variant arose apparently by an early intragenic duplication, presumably originating from an unequal crossover of two basic alleles, resulting in an Hp with an a chain of ˜14 kDa. The short and long a chains are designated as α1 and α2 respectively. Since the cysteine forming the intermolecular disulfide bond between the α chains is also duplicated, humans carrying the long variant allele exhibit a multimeric Hp phenotype (FIG. 2a). Conventional human haptoglobins have been well studied; they were discovered over 40 years ago and their role is thought to be in the plasma transport of free haemoglobin. Additionally, haptoglobin is believed to have anti-inflammatory activities, such as its decreasing effect on neutrophil metabolism, and an effect on the immune system by possibly modulating B cell proliferation and decrease antibody production. The mechanisms of the influence of haptoglobin on immune function is unknown. The potential signalling pathways by which haptoglobin is mediating its effects, and the existence of a haptoglobin receptor have not been disclosed in the prior art. However, Ghmati et al., 1996 describe a study in which haptoglobin is an alternative low-affinity ligand for CD11b/CD18 on monocyte cell lines. CD11b/CD18 is part of the integrin family and is involved in inflammatory and immunological functions. Yet another receptor molecule present on monocytes is CD163. It is identified as a member of the scavenger receptor cystein-rich superfamily (SRCR) present on cells of the monocytic family, such as most macrophages. Ritter et al., 1999 discuss the regulation, promoter structure and genomic organisation of the CD163 receptor. The precise function of CD163 is not disclosed. Furthermore, previous work on the biological function of CD163 is limited to a study on the effect of antibody-mediated crosslinking of CD163 on cultured monocytes(Van den Heuvel, M. M et al. Regulation of CD163 on human macrophages: cross-linking of CD163 induces signalling and activation. J. Leukoc.Bil. 66, 858-866 (1999). The CD163 surface ligation induces a tyrosine kinase dependent signal resulting in intracellular calcium mobilisation, inositol triphosphate production, and increased secretion of anti-inflammatory cytokines. SUMMARY The present inventors have identified CD163 as the high-affinity macrophage receptor for haptoglobin-haemoglobin complexes. They also have identified a soluble form of CD163 in plasma of normal human subjects and found a correlation between membrane bound and soluble receptor. Under normal conditions approx. 100-500 μg/l soluble CD163 is present in plasma. The present invention relates to the use of the CD163 receptor, membrane bound or soluble and/or a CD163 variant, and/or the use of haptoglobin-haemoglobin complexes in the diagnosis, prevention and/or treatment of various diseases and disorders. Accordingly, the invention describes a Hp-Hb complex, or a part thereof or a mimic thereof being operably linked to a substance, wherein the Hp-Hb complex is capable of binding CD163 and/or a CD163 variant. In the present context the term Hp-Hb complex includes a functional equivalent thereof unless expressively otherwise stated. In the present context the term “substance” means a component heterologous to the Hp-Hb complex, such as a drug, a gene, a vesicle, a vector, or the like. Further, the invention concerns the use of at least one Hp-Hb complex for the delivery of at least one drug, or at least one gene to a cell expressing a CD163 receptor and/or a CD163 receptor variant. The invention also relates to the use of at least one Hp-Hb complex, further comprising a CD163 receptor variant for the identification of at least one Hp-Hb complex in serum and/or plasma of an individual. In the present context the term CD163 receptor covers both the conventional scavenger receptor CD163 of monocytes and most tissue macrophages as well as the soluble form of CD163, sHbSR unless otherwise specified. The term CD163 is used synonymously with the term CD163 receptor. The term sHbSR is used interchangeably with soluble CD163 receptor. The term a CD163 receptor variant is used synonymously with the term CD163 variant. In another aspect, the present invention relates to a CD163 variant capable of binding at least one haptoglobin-haemoglobin (Hp-Hb) complex. In a further aspect of the invention the use of at least one CD163 variant in the manufacture of a medicament for treatment of disorders/complications related to haemolysis in an individual in need of such treatment is disclosed. Also, the invention describes the use of at least one CD163 variant for the removal of at least one Hp-Hb complex in serum and/or plasma of an individual, and the use for the determination of the haemolysis rate of an individual. Further, the use of at least one complex comprising haemoglobin and haptoglobin as a marker for a cell expressing a CD163 variant, wherein at least one of the haemoglobin or haptoglobin molecules are labelled is also described in the present invention. An object of the invention is to provide a CD163 molecule for the use as a medicament. The areas of use of a CD163 molecule according to the invention are identical to the areas of use described above for the CD163 variant. Further, a Hp-Hb complex, or a part thereof or a mimic thereof being operably linked to a substance, wherein the Hp-Hb complex is capable of binding said CD163 molecule is also within the scope of the invention. In the present context the word medicament is used in its normal meaning as a composition to be administered to an individual for prophylactic, therapeutic and/or diagnostic purposes. FIGURES FIG. 1: is an illustration of the steps involved in the Hp-Hb/CD163 binding. FIG. 2: shows examples of 2a) a haptoglobin dimer, 2b) haptoglobin multimers; 2c) Hp-Hb complexes, and 2d) a SDS-PAGE gel of mono and multimers of haptoglobin. FIG. 3: shows a CD163 molecule. FIG. 4: shows 9 different haptoglobin sequences FIG. 5: shows 4 different CD163 sequences FIG. 6: Binding of Hp-Hb to CD163. a, Illustration of the subunit organisation and disulfide bridging of the various. Hp and Hp-Hb complexes. The inset shows non-reducing SDS-PAGE of the Hp(1-1) dimer and Hp(2-2) multimers. b, Surface plasmon resonance analysis of the binding of Hp-Hb to CD163. The measurements were carried out at Hb concentrations ranging from zero to 100 μg/ml In the absence of Hp (left panel), or in the presence of 60 μg/ml of Hp(1-1) (middle panel), and 50 μg/ml Hp(2-2) (right panel). No binding was observed with either Hb or Hp alone, and saturation of the binding was obtained at 50 μg/ml Hb for both Hp phenotypes, c, Inhibition of CD163-binding of 125I-labelled Hp(1-1)-Hb (left panels) and Hp(2-2)-Hb (right panels) by polyclonal anti-CD163 IgG, non-immune rabbit IgG, EDTA (5 mM) and by various concentrations of unlabelled Hp(1-1)-Hb and Hp(2-2)-Hb complexes. CD163 was immobilised in microtiter plate wells. FIG. 7: CD163-mediated endocytosis of 125I-Hp-Hb. a, Cell-association and degradation of 125I-Hp(2-2)-Hb in mock-transfected (left panel) and CD163 cDNA-transfected CHO cells (middle panel). Addition of the lysosomal inhibitors chloroquine and leupeptin (both 100 μM) inhibited degradation leading to cellular accumulation of radioactivity (right panel). b, Inhibition of 125I-Hp-Hb uptake in CD163 cDNA-transfected CHO cells (left panel) and in CD163-expressing histiocytic lymphoma-derived SU-DHL-1 cells (right panel) Both cell types displayed a saturable uptake inhibited by anti-CD163 polyclonal IgG. The insets in a and b show anti-CD163 immunoblotting of the cells. FIG. 8: Determination of the concentration of sCD163 in the blood of a human donor. FIG. 9: Fluorescence studied in confocal microscope (example 6). FIG. 10; Sensogram of the destiny of HbSR and HbSR SRCR domain 1-6. FIG. 11: Selection of Fab antibody phage to Hp-Hb complexes and CD163. The output over input ratio, indicative of selection of clones, is depicted in panels A and C for the selections on coated Hp-Hb complexes and CD163, respectively. In the panels B and D, two representative phage ELISAs are shown in which 10 random clones from the third round of selection have been tested. Clones 3, 9 and 10 in panel B represent the Fab1 clone isolated from the Hp-Hb complex-selections and clones 8 and 9 in panel D represent the Fab18 clone isolated from the CD163 selections. In total, 50 clones from each round were screened. FIG. 12a: Binding of anti-HpHb Fab1-phage to Hp-Hb complexes, Hp and Hb. The binding to Hp-Hb complexes is represented by the circles, to Hp by the squares, to Hb by the diamonds and to BSA by the triangles. The experiment was performed in duplicate An irrelevant Fab-phage did not show binding to any of the tested antigens under these conditions (not shown). FIG. 12b: Binding of Fab1 to Hp-Hb complexes. Hp and Hb immobilized on a BIAcore sensor-chip. Binding of Fab1 to Hb is depicted in panel A, to Hp in panel B and to Hp-Hb complexes in panel C. In each case a concentration range of 0 to 200 nM Fab1 was used. FIG. 13. Fab inhibition of 125I-Hp-Hb (2:2) complex-binding to coated CD163. Curves represent the effects of increasing concentrations of anti-Hp-Hb Fab1 (diamonds), anti-CD163 Fab18 (squares) and irrelevant FabA8 (triangles) on binding of a trace amount of 125I-Hp-Hb complexes to CD163. DETAILED DESCRIPTION OF THE INVENTION In a first aspect the present invention relates to a Hp-Hb complex or a functional equivalent thereof being operably linked to a substance, said complex and/or functional equivalent thereof being capable of binding to a CD163 receptor and/or a CD163 variant. A functional equivalent of a Hp-Hb complex is to be understood as any part (or fragment) or any mimic capable of binding to a CD163 receptor. “Functional equivalency” as used in the present invention is according to one preferred embodiment established by means of reference to the corresponding functionality of a predetermined Hp-Hb fragment. In the present context the term “Hp-Hb complex” means a complex of at least one haptoglobin chain and at least one haemoglobin chain called a monomeric Hp-Hb complex. Preferably the complex comprises at least one haptoglobin chain and at least one dimeric form of haemoglobin chains. In a further preferred embodiment the complex comprises a multimeric form of haptoglobin chains such as a dimeric form, each haptoglobin chain binding at least one haemoglobin chain, preferably a dimer of haemoglobin chains. The fragment thereof should be understood to be any part of the Hp-Hb complex capable of binding to the CD163 receptor or to a variant thereof and through said binding activate uptake of the fragment and/or the-substance into the CD163 presenting cell. The mimic thereof should be understood to be any modification of the Hp-Hb complex (in the present context also called a variant of the complex) or any other molecule capable of binding to the CD163 receptor or to a variant thereof and through said binding activating uptake of the fragment and/or the substance into the CD163 presenting cell. Mimics may be peptides, peptide derivatives, antibodies, as well as non-peptide compounds, such as small organic compounds, sugars and fats. In a preferred embodiment mimics may be antibodies capable of binding to the CD163 receptor, for example in order to elicit uptake of a substance linked to the antibody. Fragments and/or mimics may be identified by combinatorial chemistry using the CD163 receptor, phase display technique or other techniques known to the person skilled in the art. The Hp-Hb complex fragment or mimic is preferably, capable of binding to a region in the SRCR domains I-IX of the CD163 receptor, such as capable of binding to a region in the SRCR domains I-VIII of the CD163 receptor, capable of binding to a region in the SRCR domains I-VII of the CD163 receptor, capable of binding to a region in the SRCR domains, I-VI of the CD163 receptor, capable of binding to a region in the SRCR domains I-V of the CD163 receptor, capable of binding to a region in the SRCR domains I-IV of the CD163 receptor, capable of binding to a region in the SRCR domains I-III of the CD163 receptor, capable of binding to a region in the SRCR domains I-II of the CD163 receptor, or a variant thereof. It is preferred that the Hp-Hb complex or a part thereof or a mimic thereof is available in a purified and/or isolated form. According to the invention the term “Hp-Hb complex” is meant to include functional equivalents of the Hp-Hb complex comprising a predetermined amino acid sequence. In the present context the term “predetermined amino acid sequence of Hp-Hb complex” relates to both the haptoglobin sequence and the haemoglobin sequence. The predetermined sequence of a haptoglobin chain may be any of the sequences shown in FIG. 4a and 4b, i.e. any of the sequences having the sequence identification in the sequence database SWISS-PROT (sp) or trEMBL (tr). sp|P00737|HPT1_HUMAN sp|P00738|HPT2_HUMAN sp|P50417|HPT_ATEGE tr|Q60574|Q60574 tr|Q61646|Q61646 sp|Q62558|HPT_MUSSA sp|P06866|HPT_RAT tr|O35086|O35086 sp|P19006|HPT_CANFA A predetermined amino acid sequence for a heamoglobin chain may be any of the sequences mentioned below together with accession No. in the sequence database SWIS-SPROT: sp|P01922|HBA_HUMAN HEMOGLOBIN ALPHA CHAIN—Homo sapiens (Human), Pan troglodytes (Chimpanzee), and Pan paniscus (Pygmy chimpanzee) (Bonobo). VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSH GSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKL LSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR sp|P02023|HBB_HUMAN HEMOGLOBIN BETA CHAIN—Homo sapiens (Human), Pan troglodytes (Chimpanzee), and Pan paniscus (Pygmy chimpanzee) (Bonobo). VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLST PDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDP ENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH sp|P02042|HBD_HUMAN HEMOGLOBIN DELTA CHAIN—Homo sapiens (Human). VHLTPEEKTAVNALWGKVNVDAVGGEALGRLLVVYPWTQRFFESFGDLSS PDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFSQLSELHCDKLHVDP ENFRLLGNVLVCVLARNFGKEFTPQMQAAYQKVVAGVANALAHKYH sp|P02096|HBG_HUMAN HEMOGLOBIN GAMMA-A AND GAMMA-G CHAINS—Homo sapiens (Human), and Pan troglodytes (Chimpanzee). GHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSS ASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDP ENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTAVASALSSRYH sp|P09105|HBAT_HUMAN HEMOGLOBIN THETA-1 CHAIN—Homo sapiens (Human). ALSAEDRALVRALWKKLGSNVGVYTTEALERTFLAFPATKTYFSHLDLSP GSSQVRAHGQKVADALSLAVERLDDLPHALSALSHLHACQLRVDPASFQL LGHCLLVTLARHYPGDFSPALQASLDKFLSHVISALVSEYR sp|P02008|HBAZ_HUMAN HEMOGLOBIN ZETA CHAIN—Homo sapiens (Human). SLTKTERTIIVSMWAKISTQADTIGTETLERLFLSHPQTKTYFPHFDLHP GSAQLRAHGSKVVAAVGDAVKSIDDIGGALSKLSELHAYILRVDPVNFKL LSHCLLVTLAARFPADFTAEAHAAWDKFLSVVSSVLTEKYR sp|P02100|HBE_HUMAN HEMOGLOBIN EPSILON CHAIN—Homo sapiens (Human). VHFTAEEKAAVTSLWSKMNVEEAGGEALGRLLVVYPWTQRFFDSFGNLSS PSAILGNPKVKAHGKKVLTSFGDAIKNMDNLKPAFAKLSELHCDKLHVDP ENFKLLGNVMVIILATHFGKEFTPEVQAAWQKLVSAVAIALAHKYH tr|Q14510|Q14510 SICKLE BETA-HEMOGLOBIN MRNA—Homo sapiens (Human). MVHLTPVEKSAVTAXWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLS TPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVD PENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH A “functional equivalents” is defined as: i) equivalents comprising an amino acid sequence capable of being recognised by an antibody also capable of recognising the predetermined amino acid sequence, and/or ii) equivalents comprising an amino acid sequence capable of binding to a receptor moiety also capable of binding the predetermined amino acid sequence, and/or iii) equivalents having at least a substantially similar or higher binding affinity to CD163 as at least a monomeric Hp-Hb complex comprising said predetermined amino acid sequence. According to the present invention a functional equivalent of a Hp-Hb complex or fragments thereof may be obtained by addition, substitution or deletion of at least one amino acid in either or both of the haptoglobin sequence and the haemoglobin sequence. Thus, a functional equivalent of the Hp-Hb complex may comprise a modification of either of the components of the complex or both. When the amino acid sequence comprises a substitution of one amino acid for another, such a substitution may be a conservative amino acid substitution. Fragments of the complex according to the present invention may comprise more than one such substitution, such as e.g. two conservative amino acid substitutions, for example three or four conservative amino acid substitutions, such as five or six conservative amino acid substitutions, for example seven or eight conservative amino acid substitutions, such as from 10 to 15 conservative amino acid substitutions, for example from 15 to 25 conservative amino acid substitution. Substitutions can be made within any one or more groups of predetermined amino acids. Examples of equivalents comprising one or more conservative amino acid substitutions including one or more conservative amino acid substitutions within the same group of predetermined amino acids, or a plurality of conservative amino acid substitutions, wherein each conservative substitution is generated by substitution within a different group of predetermined amino acids. Accordingly, mimics of the complex, or fragments thereof according to the invention may comprise, within the same mimic, or fragments thereof or among different mimics, or fragments thereof, at least one substitution, such as a plurality of substitutions introduced independently of one another. Mimics of the complex, or fragments thereof may thus comprise conservative substitutions independently of one another, wherein at least one glycine (Gly) of said mimic, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Ala, Val, Leu, and Ile, and independently thereof, mimics, or fragments thereof, wherein at least one of said alanines (Ala) of said mimics, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Gly, Val, Leu, and Ile, and independently thereof, mimics, or fragments thereof, wherein at least one valine (Val) of said mimic, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Gly, Ala, Leu, and Ile, and independently thereof, mimics, or fragments thereof, wherein at least one of said leucines (Leu) of said mimic, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Gly, Ala, Val, and Ile, and independently thereof, mimics, or fragments thereof, wherein at least one isoleucine (Ile) of said mimics, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Gly, Ala, Val and Leu, and independently thereof, mimics, or fragments thereof wherein at least one of said aspartic acids (Asp) of said mimic, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Glu, Asn, and Gln, and independently thereof, mimics, or fragments thereof, wherein at least one of said phenylalanines (Phe) of said mimics, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Tyr, Trp, His, Pro, and preferably selected from the group of amino acids consisting of Tyr and Trp, and independently thereof, mimics, or fragments thereof, wherein at least one of said tyrosines (Tyr) of said mimics, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Phe, Trp, His, Pro, preferably an amino acid selected from the group of amino acids consisting of Phe and Trp, and independently thereof, mimics, or fragments thereof, wherein at least one of said arginines (Arg) of said fragment is substituted with an amino acid selected from the group of amino acids consisting of Lys and His, and independently thereof, mimics, or fragments thereof, wherein at least one lysine (Lys) of said mimics, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Arg and His, and independently thereof, Mimics, or fragments thereof, wherein at least one of said aspargines (Asn) of said mimics, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Asp, Glu, and Gin, and independenty thereof, mimics, or fragments thereof, wherein at least one glutamine (Gin) of said mimics, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Asp, Glu, and Asn, and independently thereof, mimics, or fragments thereof, wherein at least one proline (Pro) of said mimics, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Phe, Tyr, Trp, and His, and independently thereof, mimics, or fragments thereof, wherein at least one of said cysteines (Cys) of said mimics, or fragments thereof is substituted with an amino acid selected from the group of amino acids consisting of Asp, Glu, Lys, Arg, His, Asn, Gln, Ser, Thr, and Tyr. It is clear from the above outline that the same equivalent or fragment thereof may comprise more than one conservative amino acid substitution from more than one group of conservative amino acids as defined herein above. Conservative substitutions may be introduced in any position of a preferred predetermined Hp-Hb complex of fragment thereof. It may however also be desirable to introduce non-conservative substitutions, particularly, but not limited to, a non-conservative substitution in any one or more positions. A non-conservative substitution leading to the formation of a functionally equivalent fragment of the sequences in FIG. 1 or 2 would for example i) differ substantially in polarity, for example a residue with a non-polar side chain (Ala, Leu, Pro, Trp, Val, Ile, Leu, Phe or Met) substituted for a residue with a polar side chain such as Gly, Ser, Thr, Cys, Tyr, Asn, or Gln or a charged amino acid such as Asp, Glu, Arg, or Lys, or substituting a charged or a polar residue for a non-polar one; and/or ii) differ substantially in its effect on polypeptide backbone orientation such as substitution of or for Pro or Gly by another residue; and/or iii) differ substantially in electric charge, for example substitution of a negatively charged residue such as Glu or Asp for a positively charged residue such as Lys, His or Arg (and vice versa); and/or iv) differ substantially in steric bulk, for example substitution of a bulky residue such as His, Trp, Phe or Tyr for one having a minor side chain, e.g. Ala, Gly or Ser (and vice versa). Substitution of amino acids may in one embodiment be made based upon their hydrophobicity and hydrophilicity values and the relative similarity of the amino acid side-chain substituents, including charge, size, and the like. Exemplary amino acid substitutions which take various of the foregoing characteristics into consideration are well known to those of skill in the art and include: arginine and lysine; glutamate and aspartate: serine and threonine; glutamine and asparagine; and valine, leucine and isoleucine. The addition or deletion of an amino acid may be an addition or deletion of from 2 to preferably 10 amino acids, such as from 2 to 8 amino acids, for example from 2 to 6 amino acids, such as from 2 to 4 amino acids. However, additions of more than 10 amino acids, such as additions from 10 to 200 amino acids, are also comprised within the present invention. In the discussion of deletions and additions reference is made to a monomeric form of the complex, i.e. two haemoglobin chains and one haptoglobin chain In the multimeric forms additions/deletions may be made individually in each monomer of the multimer. It will thus be understood that the invention concerns Hp-Hb complexes comprising at least one fragment capable of binding at least one CD163 receptor or a, variant thereof, including any variants and functional equivalents of such at least one fragment. The Hp-Hb complex according to the present Invention, including any functional equivalents and fragments thereof, may in one embodiment comprise less than 300 amino acid residues, such as less than 275 amino acid residues, such as less than 250 amino acid residues, such as less than 225 amino acid residues, such as less than 200 amino acid residues, such as less than 175 amino acid residues, such as less than 150 amino acid residues, such as less than 125 amino acid residues, such as less than 100 amino acid residues, such as less than 95 amino acid residues, for example less than 90 amino acid residues, such as less than 85 amino acid residues, for example less than 80 amino acid residues, such as less than 75 amino acid residues, for example less than 70 amino acid residues, such as less than 65 amino acid residues, for example less than 60 amino acid residues, such as less than 55 amino acid residues, for example less than 50 amino acid residues, such as less than 45 amino acid residues, for example less than 40 amino acid residues, such as less than 38 amino acid residues, for example less than 37 amino acid residues, such as less than 36 amino acid residues, for example less than 35 amino acid residues, such as less than 34 amino acid residues, for example less than 33 amino acid residues, such as less than 32 amino acid residues, for example less than 31 amino acid residues, such as about 30 amino acid residues, for example less than 30 amino acid residues, such as about 29 amino acid residues. The number of amino acid residues relate to the total number of amino acid residues in the complex independent of the complex being a linear amino acid sequence or a non-linear complex of amino acid sequences. A fragment comprising the CD163 binding region of native Hp-Hb complex is particularly preferred. However, the invention is not limited to fragments comprising the CD163 receptor binding region. Deletions of such fragments generating functionally equivalent fragments of the complex comprising less than the CD163 receptor binding region are also comprised in the present invention. Functionally equivalent complex peptides, and fragments thereof according to the present invention, may comprise less or more amino acid residues than CD163 receptor binding region. Fragments comprising the CD163 receptor binding region of HP-Hb complex preferably comprises regions capable of binding to the SRCR domains I-IX of the CD163 receptor, such as capable of binding to a region in the SRCR domains I-VIII of the CD163 receptor, capable of binding to a region in the SRCR domains I-VII of the CD163 receptor, capable of binding to a region in the SRCR domains I-VI of the CD163 receptor, capable of binding to a region in the SRCR domains I-V of the CD163 receptor, capable of binding to a region in the SRCR domains I-IV of the CD163 receptor, capable of binding to a region in the SRCR domains I-III of the CD163 receptor, capable of binding to a region in the SRCR domains I-II of the CD163 receptor. Fragments of the complex preferably comprises at least the heavy chain (β) of haptoglobin or a part of said chain capable of forming complex with haemoglobin. In particular the fragments may comprise a sequence corresponding to aa 103-347 of sp|P00737 in FIG. 4 or to aa 162-406 of sp|P00738. In one embodiment mimics may be understood to exhibit amino acid sequences gradually differing from the preferred predetermined sequence, as the number and scope of insertions, deletions and substitutions including conservative substitutions increases. This difference is measured as a reduction in homology between the predetermined sequence and the mimic. All functional equivalents of Hp-Hb complexes are included within the scope of this invention, regardless of the degree of homology that they show to a predetermined sequence of Hp-Hb complexes. The reason for this is that some regions of the complex are most likely readily mutatable, or capable of being completely deleted, without any significant effect on the binding activity of the resulting fragment. A functional equivalent obtained by substitution may well exhibit some form or degree of native Hp-Hb activity, and yet be less homologous, if residues containing functionally similar amino acid side chains are substituted. Functionally similar in this respect refers to dominant characteristics of the side chains such as hydrophobic, basic, neutral or acidic, or the presence or absence of steric bulk. Accordingly, in one embodiment of the invention, the degree of identity between i) a given complex equivalent capable of effect and ii) a preferred predetermined fragment, is not a principal measure of the fragment as a variant or functional equivalent of a preferred predetermined complex fragment according to the present invention. Fragments sharing at least some homology with a preferred predetermined complex fragment of at least 50 amino acids, more preferably at least 100 amino acids, are to be considered as falling within the scope of the present invention when they are at least about 40 percent homologous with the preferred predetermined Hp-Hb complex or fragment thereof, such as at least about 50 percent homologous, for example at least about 60 percent homologous, such as at least about 70 percent homologous, for example at least about 75 percent homologous, such as at least about 80 percent homologous, for example at least about 85 percent homologous, such as at least about 90 percent homologous, for example at least 92 percent homologous, such as at least 94 percent homologous, for example at least 95 percent homologous, such as at least 96 percent homologous, for example at least 97 percent homologous, such as at least 98 percent homologous, for example at least 99 percent homologous homologous with the predetermined complex fragment. In a preferred embodiment the above percentages for homology also relates to percentage identity. The Hp-Hb complex is preferably constituted of at least two different chains (sequences) wherein one chain constitutes the haptoglobin part of the complex and the other chain constitutes the haemoglobin part. A mimic of the Hp-Hb complex may however be constituted by one chain (sequence) or multimers of said chain, wherein the chain is a steric equivalent of the Hp-Hb complex. In addition to the mimics described herein, sterically similar variants may be formulated to mimic the key portions of the variant structure and that such compounds may also be used in the same manner as the variants of the invention. This may be achieved by techniques of modelling and chemical designing known to those of skill in the art. It will be understood that all such sterically similar constructs fall within the scope of the present invention. In one embodiment the Hp-Hb complex or parts thereof or mimics thereof is synthesised by automated synthesis: Any of the commercially available solid-phase techniques may be employed, such as the Merrifield solid phase synthesis method, in which amino acids are sequentially added to a growing amino acid chain. Equipment for automated synthesis of poly-peptides is commercially available from suppliers such as Applied Biosystems, Inc. of Foster City, Calif., and may generally be operated according to the manufacturer's instructions. Solid phase synthesis will enable the incorporation of desirable amino acid substitutions into any Hp-Hb complex according to the present invention. It will be understood that substitutions, deletions, insertions or any subcombination thereof may be combined to arrive at a final sequence of a functional equivalent. Insertions shall be understood to include amino-terminal and/or carboxyl-terminal fusions, e.g. with a hydrophobic or immunogenic protein or a carrier such as any polypeptide or scaffold structure capable as serving as a carrier. Hp-Hb complexes according to the invention may be synthesised both in vitro and in vivo. Methods for in vitro synthesis are well known. When synthesized in vivo, a host cell is transformed with vectors containing DNA encoding various parts of the Hp-Hb complex. A vector is defined as a replicable nucleic acid construct Vectors are used to mediate expression of the Hp-Hb complex. An expression vector is a replicable DNA construct in which a nucleic acid sequence encoding the predetermined Hp-Hb complex, or any functional equivalent thereof that can be expressed in vivo, is operably linked to suitable control sequences capable of effecting the expression of the variant, or equivalent in a suitable host. Such control sequences are well known in the art. A DNA sequence encoding the various parts of the Hp-Hb complex is meaning a DNA sequence encoding the haptoglobin part and a DNA sequence encoding the haemoglobin part. In another embodiment the DNA sequence may be one sequence encoding one peptide sequence which post-translationally is cleaved into the haptoglobin part and the haemoglobin part. In yet another embodiment one peptide constituting both parts is not cleaved, but due to post-translationally folding and/or processing functions as the complex. Accordingly, one aspect of the invention relates to a DNA sequence encoding a Hp-Hb complex as defined above, the DNA sequence may be a genomic DNA sequence, a cDNA sequence or a mixture of a genomic and a cDNA sequence. Furthermore, the invention relates to a vector comprising the DNA sequence, as well as to a cell comprising said vector, said cell being capable of expressing the DNA sequence, either as a Hp-Hb complex released into the cell culturing media, or a Hp-Hb complex anchored to the cell membrane. Cultures of cells may be derived from prokaryotic and eukaryotic cells. In principle, any higher eukaryotic cell culture is workable, whether from vertebrate or invertebrate culture but human cells are preferred. Examples of useful host cell lines E.coli, yeast, or human cell lines. Preferred host cells are eukaryotic cells known to synthesize endogenous haptoglobin and/or haemoglobin. Cultures of such host cells may be isolated and used as a source of the variant, or used in therapeutic methods of treatment, including therapeutic methods aimed at diagnostic methods carried out on the human or animal body. In order to increase the binding affinity the Hp-Hb complex or part thereof or mimic thereof is preferably dimeric. In a more preferred embodiment the the Hp-Hb complex or a part thereof or a mimic thereof is multimeric. Dimeric and multimeric relates to the number of haptoglobin monomers. The haemoglobin may be monomeric or dimeric for each haptoglobin chain.There is a correlation between the type of multimeric forms of the Hp-Hb complex and the degree of binding to a CD163 receptor or a CD163 variant of the invention. A multimeric form of a Hp-Hb complex will due to its size have an increased exposure of encountering CD163 variants as when compared to a monomeric, or even a dimeric form, and thus an increased functional affinity to CD163 variants is observed. Furthermore, the multimeric form of the complex may bind to more than one receptor on the CD163presenting cell leading to increased avidity of the binding. The multimers may be created by a common linker moiety, such as S—S bridges as in the naturally occurring haptoglobin. The common linker moiety, is preferably located so that complex-forming with haemoglobin is not disturbed. It is preferred that the common linker moiety is located in the light chain of haptoglobin. According to the invention the Hp-Hb complex, or a part thereof being operably linked to a substance as described above may be for the use as a medicament. Such medicament may operate through a method, wherein the Hp-Hb complex or a part thereof is used in a method of treatment of an individual, comprising the steps of: i) providing a Hp-Hb complex, or a part thereof or a mimic thereof capable of binding to the CD163 receptor and/or the CD163 variant, ii) operably linking a substance as defined above to the Hp-Hb complex or a part thereof or mimic thereof, iii) administering the medicament comprising the substance operably linked to the Hp-Hb complex to an individual in need thereof. The term operably linked means that the substance is coupled or bound to the complex in a manner so that the substance is transported to the cell presenting a CD163 receptor or a CD163 variant, whereafter the substance may be released from the complex if appropriate. Due to the binding of the complex or fragment or mimic thereof to the CD163 receptor and/or a CD163 variant the substance comprised in or bound to the Hp-Hb complex is either taken up by the CD163 presenting cells or at least located in the environment close to the cells. Thereby it is possible to concentrate the substance in or around the cell presenting the CD163 receptor. A test for analysing optional uptake is described below in Example 4. In one embodiment of the invention the Hp-Hb complex, or a part thereof may be operably linked to a substance, such as a medicament, a gene, a vesicle, vector or the like. The medicament may be any medicament for which it is desirable to target the drug to a particular tissue or particular cells. In particular the medicament is an antimicrobial agent or a cancer drug. The medicament is preferably a medicament against diseases in relation to monocytes, such as macrophages. In particular the invention relates to a complex being operably linked to a anti-HIV drug. In another embodiment the substance is a medicament against lymphomas, such as histiocytic lymphomas. In yet another embodiment the substance may stimulate the macrophages to produce interleukin 6. In a further embodiment the substance is an antigen for vaccine purposes. In another embodiment the substance of the Hp-Hb complex, or a functional equivalent thereof comprises a gene, i.e. a gene construct. The gene may be any gene encoding a particular biological function. For example the gene may comprise a nucleic acid, such as PNA, LNA, DNA or RNA, or the gene may comprise cDNA. The gene may also comprise less than full length genes or cDNAs, such as fragment thereof. The Hp-Hb complex comprising a gene may be used in gene-delivery therapy, whereby the gene is taken up by the cell presenting the CD163 receptor or a variant thereof. The constructs can be introduced as one or more DNA molecules or constructs. The constructs are prepared in conventional ways, where the genes and regulatory regions may be isolated, as appropriate, ligated, cloned in an appropriate cloning host, analyzed by restriction or sequencing, or other convenient means. Using PCR, individual fragments including all or portions of a functional unit may be isolated, where one or more mutations may be introduced using “primer repair”, ligation, in vitro mutagenesis, etc. as appropriate. The construct(s) once completed and demonstrated to have the appropriate sequences may then be introduced into host cells by any convenient means, as discussed in more detail below. The constructs may be introduced as a single DNA molecule encoding all of the genes, or different DNA molecules having one or more genes. The constructs may be introduced simultaneously or consecutively, each with the same or different markers. The gene may be linked to the complex as such or protected by any suitable system normally used for transfection such as viral vectors or artificial viral envelope, liposomes or micellas, wherein the system is linked to the complex. Numerous techniques for introducing DNA into eukaryotic cells are known to the skilled artisan. Often this is done by means of vectors, and often in the form of nucleic acid encapsidated by a (frequently virus-like) proteinaceous coat. Gene delivery systems may be applied to a wide range of clinical as well as experimental applications. Vectors containing useful elements such as selectable and/or amplifiable markers, promoter/enhancer elements for expression in mammalian, particularly human, cells, and which may be used to prepare stocks of construct DNAs and for carrying out transfections are well known in the art. Many are commercially available. Various techniques have been developed for modification of target tissue and cells in vivo. A number of virus vectors, discussed below, are known which allow transfection and random integration of the virus into the host. See, for example, Dubensky et al. (1984) Proc. Natl. Acad. Sci. USA 81:7529-7533; Kaneda et al., (1989) Science 243-375-378; Hiebert et al. (1989) Proc. Natl. Acad. Sci. USA 86:3594-3598; Hatzoglu et al., (1990) J. Biol. Chem. 265:17285-17293; Ferry et al (1991) Proc. Natl. Acad. Sci. USA 88:8377-8381. Routes and modes of administering the vector include injection, e.g intravasculary or intramuscularly, inhalation, or other parenteral administration. Advantages of adenovirus vectors for human gene therapy include the fact that recombination is rare, no human malignancies are known to be associated with such viruses, the adenovirus genome is double stranded DNA which can be manipulated to accept foreign genes of up to 7.5 kb in size, and live adenovirus is a safe human vaccine organisms. Another vector which can express the DNA molecule of the present invention, and is useful in gene therapy, particularly in humans, is vaccinia virus, which can be rendered non-replicating (U.S. Pat Nos. 5,225,336; 5,204,243: 5,155,020; 4,769,330). Based on the concept of viral mimicry, artificial viral envelopes (AVE) are designed based on the structure and composition of a viral membrane, such as HIV-1 or RSV and used to deliver genes into cells in vitro and in vivo. See, for example, U.S. Pat. No. 5,252,348, Schreier H. et al., J. Mol. Recognit, 1995, 8:59-62; Schreier H et al., J. Biol. Chem., 1994, 269:9090-9098; Schreier, H., Pharm. Acta Helv. 1994, 68:145-159; Chander, R et al. Life Sci., 1992, 50:481-489, which references are hereby incorporated by reference in their entirety. The envelope is preferably produced in a two-step dialysis procedure where the “naked” envelope is formed initially, followed by unidirectional insertion of the viral surface glycoprotein of interest. This process and the physical characteristics of the resulting AVE are described in detail by Chander et al., (supra). Examples of AVE systems are (a) an AVE containing the HIV-1 surface glycoprotein gp160 (Chander et al., supra; Schreier et al., 1995, supra) or glycosyl phosphatidylinositol (GPI)-linked gp120 (Schreier et al., 1994, supra), respectively, and (b) an AVE containing the respiratory syncytial virus (RSV) attachment (G) and fusion (F) glycoproteins (Stecenko, A. A. et al., Pharm. Pharmacol. Lett. 1:127-129 (1992)). Thus, vesicles are constructed which mimic the natural membranes of enveloped viruses in their ability to bind to and deliver materials to cells bearing corresponding surface receptors. AVEs are used to deliver genes both by intravenous injection and by instillation in the lungs. For example, AVEs are manufactured to mimic RSV, exhibiting the RSV F surface glyco-protein which provides selective entry into epithelial cells. F-AVE are loaded with a plasmid coding for the gene of interest, (or a reporter gene such as CAT not present in mammalian tissue). The AVE system described herein in physically and chemically essentially identical to the natural virus yet is entirely “artificial”, as it is constructed from phospholipids, cholesterol, and recombinant viral surface glycoproteins. Hence, there is no carry-over of vital genetic information and no danger of inadvertant viral infection. Construction of the AVEs in two independent steps allows for bulk production of the plain lipid envelopes which, in a separate second step, can then be marked with the desired viral glycoprotein, also allowing for the preparation of protein cocktail formulations if desired. Another delivery vehicle for use in the present invention are based on the recent description of attenuated Shigella as a DNA delivery system (Sizemore, D. R. et al., Science 270:299-302 (1995), which reference is incorporated by reference in its entirety). This approach exploits the ability of Shigellae to enter epithelial cells and escape the phagocytic vacuole as a method for delivering the gene construct into the cytoplasm of the target cell. Invasion with as few as one to five bacteria can result in expression of the foreign plasmid DNA delivered by these bacteria. A preferred type of mediator of nonviral transfection in vitro and in vivo is cationic (ammonium derivatized) lipids. These positively charged lipids form complexes with negatively charged DNA, resulting in DNA charged neutralization and compaction. The complexes endocytosed upon association with the cell membrane, and the DNA somehow escapes the endosome, gaining access to the cytoplasm, Cationic lipid-DNA complexes appear highly stable under normal conditions. Studies of the cationic lipid DOTAP suggest the complex dissociates when the inner layer of the cell membrane is destabilized and anionic lipids from the inner layer displace DNA from the cationic lipid. Several cationic lipids are available commercially. Two of these, DMRI and DC-cholesterol, have been used in human clinical trials. First generation cationic lipids are less efficient than viral vectors. For delivery to lung, any inflammatory responses accompanying the liposome administration are reduced by changing the delivery mode to aerosol administration which distributes the dose more evenly. The gene may be any gene appropriately expressed by the CD163 presenting cells. In one embodiment the gene may be a gene for CD163 as a gene therapy for individuals having reduced CD-163 expression. In another embodiment the gene encodes an antigen for as a gene vaccination. In any situation it may be an advantage that macrophages do not multiply whereby this kind of gene therapy is an appropriate form of temporary gene therapy. The gene therapy approach can be utilized in a site specific manner to deliver a retroviral vector to the tissue or organ of choice. Thus, for example, a catheter delivery system can be used (Nabel, E. G. et al., Science 244:1342 (1989)). Such methods, using either a retroviral vector or a liposome vector, is particularly useful to deliver the gene to a blood vessel wall. Other virus vectors may also be used, in particular for human gene therapy, including recombinant adenovirus vectors, A nontoxic and efficient method has recently been reported based on the Sendai virus, also known as hemagglutinating virus of Japan (HVJ). HVJ-liposome-mediated gene transfer is performed Morishita R et al., Hypertension (1993) 21:894-89. Further, the substance of the Hp-Hb complex, or a part thereof may also comprise a tracer or a marker, such as chromophores; fluorphores, biotin, isotopes, enzymes, for identifying the cells presenting the CD163 receptor or a variant thereof. Thereby Hp-Hb complex may be used for diagnostic purposes as well. In one embodiment the Hp-Hb complex or fragment thereof or mimic thereof being operably linked to a substance is capable of binding a CD163 variant only, in order to avoid binding to the naturally occurring CD163 receptor on macrophages. Thereby it is possible to direct a substance to a subgroup of cells presenting the CD163 variant only. It is another object of the present invention to use a CD163 molecule as a medicament. Use of a CD163 molecule in the manufacture of a medicament for treatment of haemolysis in an individual in need of such treatment. There are a number of application fields, wherein one is the use of a CD163 molecule for the removal of at least one Hp-Hb complex in serum and/or plasma of an individual. A second application is the use of a CD163 molecule for the determination of the haemolysis rate of an individual. Further, the use of at least one complex comprising haemoglobin and haptoglobin as a-marker for a cell, such as a macrophage expressing a CD163 molecule, wherein at least one of the haemoglobin or haptoglobin molecules are labelled is yet another application area. According to the invention the term “CD163 variant” is meant to include functional equivalents of CD163, or a fragment of CD163, said CD163 comprising a predetermined amino acid sequence. Thus, a CD163 variant is different from native CD163. A “variant” is defined as: iv) variants comprising an amino acid sequence capable of being recognised by an antibody also capable of recognising the predetermined amino acid sequence, and/or v) variants comprising an amino acid sequence capable of binding to a Hp-Hb complex also capable of binding the predetermined amino acid sequence, and/or vi) variants having at least a substantially similar binding affinity to at least one Hp-Hb complex as said predetermined amino acid sequence. By the term “predetermined amino acid sequence” is meant any of the amino acid sequences depicted in FIG. 5a and 5b, i.e. any of the sequences for CD163 having the following sequence identification in sequence database trEMBL: tr|Q07898|Q07898 tr|Q07901|Q07901 tr|Q07900|Q07900 tr|Q07899|Q07899 “Functional equivalency” as used in the present invention is according to one preferred embodiment established by means of reference to the corresponding functionality of a predetermined CD163 fragment. According to the present invention a functional equivalent of a CD163 variant or fragments thereof may be obtained by addition, substitution or deletion of at least one amino acid. When the amino acid sequence comprises a substitution of one amino acid for another, such a substitution may be
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