Abstract
A procedure is described for purification of phosphoglucomutase [EC 2. 7. 5. 1] from beef liver. The purified enzyme preparation was homogeneous on the analysis of ultracentrifugation and zone electrophoresis. The molecular weight was determined to be 64, 000 by the meniscus depletion method.
The amino acid composition of liver phosphoglucomutase was very similar to that of the rabbit muscle enzyme.
The reaction mechanism of liver phosphoglucomutase was examined kinetically. The results of kinetical experiments strongly suggested that the reaction of liver phosphogluco-mutase proceeds via “ping-pong” mechanism.
Liver phosphoglucomutase activity was remarkably inhibited by Fru-1, 6-P2, glycerate-2, 3-P2 and glycerate-1, 3-P2. Role of the bisphosphate compounds on the control of carbohydrate metabolism is discussed.
