VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Kinetic properties of partially purified glucosephosphate dehydrogenase of human erythrocytes

   
Batishchev A.I., Lamzina N.V., Cherniak N.B.
PubMed Id: 16398
Year: 1976  Volume: 22  Issue: 3  Pages: 351-356
Partially purified glucose-6-phosphate dehydrogenase was isolated from small amounts of human erythrocytes (15-20 ml). The Km value for glucose-6-phosphate was 35.0 +/- 3.0 micronM, the Km for NADP was 4.27 +/- 0.3 micronM. The optimal activity of the enzyme was at pH 9.0. Glucose-6-phosphate dehydrogenase, dialyzed in presence of 1-10(-5) M NADP, had critical temperature about 52 degrees within 10 min of incubation; without NADP it was at 45 degrees. The method for isolation and purification of the enzyme was modified.
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Batishchev, A. I., Lamzina, N. V., Cherniak, N. B. (1976). Kinetic properties of partially purified glucosephosphate dehydrogenase of human erythrocytes. Voprosy Meditsinskoi Khimii, 22(3), 351-356.
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