Title : Human erythrocyte glucose 6-phosphate dehydrogenase. Influence of coenzyme derivatives on thermostability and kinetic properties.

Pub. Date : 1975 Mar-Apr

PMID : 239915






9 Functional Relationships(s)
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1 A number of derivatives of NADP(H) were tested with respect to their effectiveness in interacting with tetrameric glucose 6-phosphate dehydrogenase (G6PD) retaining only the fraction of "structural" coenzyme (4 moles NADP). NADP glucose-6-phosphate dehydrogenase Homo sapiens
2 A number of derivatives of NADP(H) were tested with respect to their effectiveness in interacting with tetrameric glucose 6-phosphate dehydrogenase (G6PD) retaining only the fraction of "structural" coenzyme (4 moles NADP). NADP glucose-6-phosphate dehydrogenase Homo sapiens
3 A number of derivatives of NADP(H) were tested with respect to their effectiveness in interacting with tetrameric glucose 6-phosphate dehydrogenase (G6PD) retaining only the fraction of "structural" coenzyme (4 moles NADP). NADP glucose-6-phosphate dehydrogenase Homo sapiens
4 A number of derivatives of NADP(H) were tested with respect to their effectiveness in interacting with tetrameric glucose 6-phosphate dehydrogenase (G6PD) retaining only the fraction of "structural" coenzyme (4 moles NADP). NADP glucose-6-phosphate dehydrogenase Homo sapiens
5 Interaction was probed by two parameters: a) increased thermostability of G6PD activity, measured as the difference in the corresponding transition temperature (Tm) of samples containing and lacking the NADP derivatives, respectively; b) competitive inhibition toward NADP, expressed a Ki values. NADP glucose-6-phosphate dehydrogenase Homo sapiens
6 Interaction was probed by two parameters: a) increased thermostability of G6PD activity, measured as the difference in the corresponding transition temperature (Tm) of samples containing and lacking the NADP derivatives, respectively; b) competitive inhibition toward NADP, expressed a Ki values. NADP glucose-6-phosphate dehydrogenase Homo sapiens
7 These data show that the adenosine moiety of NADP is more critically involved than the nicotinamide portion in the interaction with human G6PD. Adenosine glucose-6-phosphate dehydrogenase Homo sapiens
8 These data show that the adenosine moiety of NADP is more critically involved than the nicotinamide portion in the interaction with human G6PD. NADP glucose-6-phosphate dehydrogenase Homo sapiens
9 These data show that the adenosine moiety of NADP is more critically involved than the nicotinamide portion in the interaction with human G6PD. Niacinamide glucose-6-phosphate dehydrogenase Homo sapiens