嗜热和嗜温6-磷酸葡萄糖酸脱氢酶在8M尿素作用下的变性

Denaturation of thermophilic and mesophilic 6-phosphogluconate dehydrogenase by 8M urea.

作者信息

Veronese F M, Boccu E, Fontana A

出版信息

Int J Pept Protein Res. 1975;7(4):341-3. doi: 10.1111/j.1399-3011.1975.tb02450.x.

DOI:10.1111/j.1399-3011.1975.tb02450.x

Abstract

The denaturation reaction of 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP oxidoreductase (decarboxylating EC 1.1.1.44) from B. Stearothermophilus and E. coli in 8 M urea has been compared. The rates of denaturation were evaluated from the fluorescence quenching that occurs at 334 nm. The thermophilic enzyme has been found about ten times more resistant to the action of the denaturating agent, and showed a biphasic denaturation process, whereas the E. coli enzyme followed a single first-order kinetics.

摘要

已对嗜热脂肪芽孢杆菌和大肠杆菌的6-磷酸葡萄糖酸脱氢酶（6-磷酸-D-葡萄糖酸：NADP氧化还原酶（脱羧，EC 1.1.1.44））在8 M尿素中的变性反应进行了比较。通过在334 nm处发生的荧光猝灭来评估变性速率。已发现嗜热酶对变性剂作用的抗性约为大肠杆菌酶的十倍，并且呈现出双相变性过程，而大肠杆菌酶遵循单一的一级动力学。

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