Abstract
Phosphoglucose isomerase from Aspergillus niger was purified about fiftyfold by ammonium sulphate fractionation and treatment with calcium phosphate gel. The properties and kinetics of the enzyme are described. The enzyme resembled the muscle phosphoglucose isomerase in not requiring metal ions for activation but differed in showing no inhibition with phosphate. The enzyme showed maximum activity between pH 7.8 to 8.0 as compared with the optimum pH 9.0 shown by the muscle enzyme.
Publisher
Canadian Science Publishing
Cited by
4 articles.
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