Abstract
Abstract A procedure is described for the purification of glucose 6-phosphate dehydrogenase (d-glucose 6-phosphate: NADP oxidoreductase, EC 1.1.1.49) from wild type Neurospora crassa. A 2400-fold purification was achieved with a 10% yield and an average specific activity of 470. The glucose 6-phosphate and NADP Michaelis constants were determined, as well as the optimal pH for activity. The analogues, 2-deoxyglucose 6-phosphate and galactose 6-phosphate, were utilized as substrates in place of glucose 6-phosphate. No reaction was observed when NAD was substituted for NADP. The amino acid composition and extinction coefficient are given.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Paper version not known
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
