Partial purification and properties of glucose-6-phosphate dehydrogenase from Macracanthorhynchus hirudinaceus (Acanthocephala)

Abstract

1.1. Glucose-6-phosphate dehydrogenase (E.C.1.1.1.49) in Macracanthorhynchus hirudinaceus was purified 321-fold. The techniques used for purification include ammonium sulfate fractionation, calcium phosphate gel absorption and DEAE cellulose absorption.2.2. Properties of the partial purified enzyme are: (a) an optimal temperature of 40°C, (b) an optimal pH of 7·6, (c) an optimal requirement for MgCl2 of 0·033 M and (d) a Michaelis constant of 1 × 10−4 M for d-glucose-6-phosphate. The enzyme was unstable during dialysis, with a linear loss of activity.