THREONINE-SENSITIVE HOMOSERINE DEHYDROGENASE AND ASPARTOKINASE ACTIVITIES OF ESCHERICHIA COLI K12 - SUBUNIT STRUCTURE OF PROTEIN CATALYZING 2 ACTIVITIES

被引：35

作者：

TRUFFABA.P

VANRAPEN.R

JANIN, J

GROS, C

COHEN, GN

机构：

[1] Laboratoire d'Enzymologie, CN.R.S

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

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1969年 / 7卷 / 03期

关键词：

D O I：

10.1111/j.1432-1033.1969.tb19623.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 threonine sensitive activities aspartokinase I and homoserine dehydrogenase I is composed of six subunits of a molecular weight 60,000. Furthermore, quantitative determination of the N‐terminal amino acids indicates the presence of six methionine residues per mole of native enzyme (mol. wt. 360,000). Equilibrium sedimentation studies of N‐ethylmaleimide treated protein shows that its six disulfide bridges, revealed by chemical analysis, are intra‐chain. Fingerprints of tryptic digests of the protein fail to reveal any difference between the subunits. Copyright © 1969, Wiley Blackwell. All rights reserved

引用

页码：401 / &

共 29 条

[1]

BISERTE G, 1951, B SOC CHIM BIOL, V33, P50

[2]

BRENNER M, 1961, EXPERIENTIA, V17, P45

[3] EVIDENCE FOR POSSIBLE NONSPECIFIC REACTIONS BETWEEN N-ETHYLMALEIMIDE AND PROTEINS [J].