PURIFICATION AND CHARACTERIZATION OF FULLY DEUTERATED ENZYMES

被引：23

作者：

ROKOP, S

GAJDA, L

PARMERTER, S

CRESPI, HL

KATZ, JJ

机构：

[1] Chemistry Division, Argonne National Laboratory, Argonne

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 191卷 / 03期

关键词：

D O I：

10.1016/0005-2744(69)90365-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two fully deuterated enzymes, a bacterial alkaline phosphatase and a plant ribonuclease, have been isolated in a high degree of purity. Kinetic measurements and thermal studies indicate only slight differences in the tertiary structure of the fully deuterated enzymes as compared to the ordinary enzymes. However, the deuterated alkaline phosphatase shows a decreased rate of catalysis. © 1969.

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页码：707 / +

页数：1

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