THREONINE-SENSITIVE HOMOSERINE DEHYDROGENASE AND ASPARTOKINASE ACTIVITIES OF ESCHERICHIA COLI K12 .4. ISOLATION MOLECULAR WEIGHT AMINO ACID ANALYSIS AND BEHAVIOUR OF SULFHYDRYL GROUPS OF PROTEIN CATALYZING 2 ACTIVITIES

被引：93

作者：

TRUFABAC.P

VANRAPEN.R

JANIN, J

GROS, C

COHEN, GN

机构：

[1] Laboratoire d'Enzymologie du C. N. R. S. F-91, Gif-Sur-Yvette

[2] Laboratoire de Biochimie, Faculté des Sciences, Orsay

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1968年 / 5卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1968.tb00339.x

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：

The complex protein carrying the two theronine sensitive activities aspartokinase I and homoserine dehydrogenase I has been obtained in a homogenous state from extracts of Escherichia coli K 12. The molecular weight of the protein has been determined by sedimentation equilibrium to be 360,000 dalton. The amino acid composition is given. Titration of sulfhydryl groups by 5–5′‐dithiobis‐(2‐nitrobenzoic)acid leads to an estimation of 16 of 18 reactive cysteines per mole of the protein, all of which can be protected by addition of the allosteric inhibitor, L‐theronine. Copyright © 1968, Wiley Blackwell. All rights reserved

引用

页码：73 / &

共 31 条

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