PURIFICATION AND PROPERTIES OF RAT LIVER HISTIDASE

被引：21

作者：

CORNELL, NW

VILLEE, CA

机构：

[1] Department of Biological Chemistry, Harvard Medical School, Boston, MA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1968年 / 167卷 / 01期

关键词：

D O I：

10.1016/0005-2744(68)90287-8

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：

Rat liver histidase (l-histidine ammonia-lyase, EC 4.3.1.3) has been purified 200-fold. The final preparation was estimated to be about 80% pure and was used to evaluate cofactor requirements and other reaction parameters. Histidase has a molecular weight of 226 000, a Km for histidine of 2.0 · 10-3 M, and a pH optimum of 8.8-9.2. The enzyme is stimulated by glutathione although the latter appears to function as a bivalent anion, not as a sulfhydryl-protecting reagent. Histidase is inhibited by versene, and the inhibition is effectively reversed by both manganese and zinc ions; magnesium is slightly less effective in this regard. Some physiological implications of the histidase reaction are discussed. © 1968.

引用

页码：172 / &

共 18 条

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