PROPERTIES OF CRYSTALLINE AMINO ACID POLYMERIZATION FACTORS FROM ESCHERICHIA COLI - BINDING OF G TO RIBOSOMES

被引：42
作者：
PARMEGGIANI, A
GOTTSCHALK, EM
机构：
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 35卷 / 06期
关键词：
D O I：
10.1016/0006-291X(69)90703-7
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：
In the past few years a great number of independent reports have indicated the requirement of the protein factors G and T for ribosomal polypeptide synthesis in the in vitro system from E. coli (1-9). With the availability of electrophoretically homogeneous, crystalline G factor (7), the importance of studying the direct interaction of this enzyme with ribosomes became evident. Moldave and co-workers already observed in the rat liver system that aminoacyltransferase II - comparable to G - binds to ribosomes in the presence of a guanine nucleotide (10, 11). In this communication, we extend our observations (12, 13) on the formation of a G-ribosome complex. © 1969.
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页码：861 / +
页数：1
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