<prompt> Low haptoglobin in haemorrhage is masked by concurrent presence ofMalnutritionPregnancyObstructive biliary diseaseLiver parenchymal disease  <response>: D i.e Liver parenchymal disease Haptoglobin Hp binds extracorpuscular i.e. extracellular hemoglobin Hb, preventing free Hb from entering the kidney. Hp-Hb complex is removed from plasma by haptocytes. Levels of haptoglobin falls rapidly in situations where hemoglobin is constantly being released from RBC such as occurs in hemolytic anemia haemorrhage. But in case of parenchymal liver disease, Hp-Hb complex removal is deranged so reduction in haptoglobin level is masked. Haptoglobin It is a plasma glycoprotein that binds extracapsular hemoglobin Hb in a tight non-covalent complex. Its amount ranges from 40mg- 180 mg of hemoglobin binding capacity deciliter. Only 10 of degraded hemoglobin is released in circulation i.e. extra corpuscular the remaining 90 is present in old damaged RBCs, which are degraded by histiocytic system. Free Hb molecular mass 65KDa passes through glomerulus and precipitate in tubules. However, after binding with haptoglobin 90 KDa the Hb-Hp complex 155KDa becomes too large to pass through glomerulus. So the function of haptoglobin is to prevent loss of free hemoglobin into kidney and conserve the valuable iron present in hemoglobin, which would otherwise be lost to the body. Humans have 3 polymorphic forms, ka Hp 1-1, Hp 2-1, Hp 2-2. Low levels of haptoglobins are found in patients with hemolytic anemia. This is explained by the fact that where the life of Hp is 5 days, the t12 of Hb-Hp complex is 90 minutes, the complex being rapidly removed by hepatocytes. So when the hepatoglobin is bound to Hb, it is cleared from plasma about 80 times faster than normally. Hb is an acute phase protein is elevated in variety of inflammatory states. Haptoglobin related protein binds hemoglobin; hemopexin binds free heme; and albumin binds metheme ferric heme 