Glucose‐6‐phosphate dehydrogenase is purified from C57BL mouse liver to a specific activity of 116 units/mg protein. The molecular weight of the main active unit is 121000 and it is composed of three interconvertible subforms, as revealed by acrylamide electrophoresis. The main active unit is composed of two subunits of molecular weight 62000, and may aggregate to form higher oligomers. Amino acid composition and dependence of rate on pH and substrate concentration are reported. The kinetic data suggest the existence of two types of active sites with separate sets of Km and V values. The electrophoretic and kinetic properties of the enzyme from induced and non‐induced liver homogenates are compared.
|Number of pages||9|
|Journal||European Journal of Biochemistry|
|State||Published - Jun 1974|