PURIFICATION AND PROPERTIES OF PYRUVATE-KINASE FROM HUMAN LUNG

被引：29

作者：

CORCORAN, E ^{[1
]}

PHELAN, JJ ^{[1
]}

FOTTRELL, PF ^{[1
]}

机构：

[1] NATL UNIV IRELAND, UNIV COLL GALWAY, DEPT BIOCHEM, GALWAY, IRELAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1976年 / 446卷 / 01期

关键词：

D O I：

10.1016/0005-2795(76)90101-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：

Pyruvate kinase was purified to homogeneity from human lung and characterized kinetically. The enzyme has a MW of 250,000 and a subunit MW of 62,000. An amino acid analysis of the pyruvate kinase followed by peptide mapping of a tryptic digest confirmed that the enzyme contained 4 identical subunits.

引用

页码：96 / 104

页数：9

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