2 FORMS OF PYRUVATE-KINASE IN ESCHERICHIA-COLI - COMPARISON OF CHEMICAL AND MOLECULAR-PROPERTIES

被引：29

作者：

VALENTINI, G ^{[1
]}

IADAROLA, P ^{[1
]}

SOMANI, BL ^{[1
]}

MALCOVATI, M ^{[1
]}

机构：

[1] UNIV PAVIA,FAC MED,INST CHIM BIOL,I-27100 PAVIA,ITALY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 570卷 / 02期

关键词：

(E. coli); Amino acid analysis; Pyruvate kinase; Subunit structure; Tryptic digestion;

D O I：

10.1016/0005-2744(79)90145-1

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 two forms of pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) present in Escherichia coli have been purified from the same cultures and crystallized. A modified procedure for the purification of type I pyruvate kinase is described. Molecular weight, subunit structure, amino acid composition, NH2-terminal amino acid, maps of tryptic peptides and conditions for crystallization have been determined for the two forms. A comparison of these data shows that the two forms are different proteins, each being a tetramer of identical subunits. © 1979.

引用

页码：248 / 258

页数：11

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