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. 1976 Sep;58(3):393–397. doi: 10.1104/pp.58.3.393

Purification and Characterization of Glucose Dehydrogenase from a Heterotrophically Grown Blue-Green Alga 1

Warren M Pulich a, Chase Baalen a, Janet L Gibson b, F Robert Tabita b
PMCID: PMC542253  PMID: 16659685

Abstract

NADP- and NAD-dependent glucose dehydrogenase was partially purified from a dark-grown blue-green alga (endophytic Nostoc strain MAC). Polyacrylamide gel electrophoresis established that a single protein possessed dual activity for either NADP or NAD. No other electron acceptor substituted for pyridine nucleotides and no evidence for a flavin prosthetic group was found. Although the Km for NADP was 8.8 μm and for NAD 328 μm, the enzyme was equally active with NAD or NADP at saturating levels of substrates. The enzyme was similar to previously described glucose dehydrogenase in that it had a high Km for glucose (18-20 mm at 35 C) and an alkaline pH optimum of 7.6 to 9.4.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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