in an enzyme that is more efficient, or one that can catalyse a slightly different chemical reaction, in which case the mutation may cause an increase in fitness, and be favoured by natural selection. Examples An example of an isozyme is glucokinase, a variant of hexokinase which is not inhibited by glucose 6-phosphate. Its different regulatory features and lower affinity for glucose (compared to other hexokinases), allow it to serve different functions in cells of specific organs, such as control of insulin release by the beta cells of the pancreas, or initiation of glycogen synthesis by liver cells. Both these processes must only occur when glucose is abundant. 1.) The enzyme lactate dehydrogenase is a tetramer made of two different sub-units, the H-form and the M-form. These combine in different combinations depending on the tissue: 2.) Isoenzymes of creatine phosphokinase: Creatine kinase (CK) or creatine phosphokinase (CPK) catalyses the interconversion of phospho creatine to creatine . CPK exists in 3 isoenzymes. Each isoenzymes is a dimer of 2 subunits M (muscle), B (brain) or both 3.) Isoenzymes of alkaline phosphatase: Six isoenzymes have been identified. The enzyme is a monomer, the isoenzymes are due to the differences in the carbohydrate content (sialic acid residues). The most important ALP isoenzymes are α1-ALP, α2-heat labile ALP, α2-heat stable ALP, pre-β ALP and γ-ALP. Increase in α2-heat labile ALP suggests hepatitis whereas pre-β ALP indicates bone diseases. Distinguishing isozymes Isozymes (and allozymes) are variants of the same enzyme. Unless they are identical in their biochemical properties, for example their substrates and enzyme kinetics, they may be distinguished by a biochemical assay. However, such differences are usually subtle, particularly between allozymes which are often neutral variants. This subtlety is to be expected, because two enzymes that differ significantly in their function are unlikely to have been identified as isozymes. While isozymes may be almost identical in function, they may differ in other ways. In particular, amino acid substitutions that change the electric charge of the enzyme are simple to identify by gel electrophoresis, and this forms the basis for the use of isozymes as molecular markers. To identify isozymes, a crude protein extract is made by grinding animal or plant tissue with an extraction buffer, and the components of extract are separated according to their charge by gel electrophoresis. Historically, this has usually been done using gels made from potato starch, but acrylamide gels