A SOLUBLE ENZYME FROM ESCHERICHIA COLI WHICH CATALYZES TRANSFER OF LEUCINE AND PHENYLALANINE FROM TRNA TO ACCEPTOR PROTEINS

被引：48

作者：

LEIBOWITZ, MJ

SOFFER, RL

机构：

[1] Albert Einstein College, Medicine Department, Molecular Biology Division of Biological Sciences Bronx

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 36卷 / 01期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

D O I：

10.1016/0006-291X(69)90647-0

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：

A soluble enzyme which catalyzes the transfer of leucine and phenylalanine from tRNA to protein has been partially purified from Escherichia coli. No activity is observed with other amino acyl tRNAs. The transfer reaction does not require magnesium ions but does require a monovalent cation and an acceptor protein such as bovine serum albumin. © 1969.

引用

页码：47 / +

页数：1

共 10 条

[1]

KAJI A, 1965, J BIOL CHEM, V240, P1192

[2]

KAJI A, 1965, J BIOL CHEM, V240, P1185

[3]

LOWRY OH, 1951, J BIOL CHEM, V193, P265

[4] A CONVENIENT, RAPID AND SENSITIVE METHOD FOR MEASURING THE INCORPORATION OF RADIOACTIVE AMINO ACIDS INTO PROTEIN [J].