PURIFICATION AND PROPERTIES OF AGMATINE IMINOHYDROLASE FROM GROUNDNUT COTYLEDONS

被引：18

作者：

SINDHU, RK ^{[1
]}

DESAI, HV ^{[1
]}

机构：

[1] MAHARAJA SAYAJIRAO UNIV BARODA,DEPT BIOCHEM,BARODA 390002,GUJARAT,INDIA

来源：

PHYTOCHEMISTRY | 1979年 / 18卷 / 12期

关键词：

agmatine iminohydrolase; Arachis hypogea; groundnut; kinetics; Leguminosae; polyamines; purification;

D O I：

10.1016/S0031-9422(00)82706-5

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：

Agmatine iminohydrolase was purified ca 375-fold from groundnut cotyledons. The enzyme exhibited an optimum pH between 5.5 and 8.5 and the energy of activation was 22 kcal/mol. The Km for agmatine was (7.57 ± 0.77) × 10-4 M. The enzyme was inhibited by tryptamine, putrescine, cadaverine, spermidine and spermine. Inhibition by cadaverine and spermidine was competitive. The Ki values for cadaverine and spermidine were 4.1 × 10-3 and 7.5 × 10-4 M, respectively. © 1979.

引用

页码：1937 / 1938

页数：2

共 8 条

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