Affiliation:
1. Department of Microbiology, University of Illinois, Urbana, Illinois 61801
Abstract
Twelve of the proteins from the 30
S
ribosome of
Bacillus stearothermophilus
were isolated by preparative disc electrophoresis. Amino acid analyses of these proteins showed them to be different from each other. The gross amino acid composition of 30
S
ribosomal protein from
B. stearothermophilus
and
Escherichia coli
are virtually identical. A number of the proteins of
B. stearothermophilus
had electrophoretic mobilities similar or identical to 30
S
ribosomal proteins of
E. coli
. However, there was little similarity between the two organisms in amino acid composition of individual proteins. There were no unusual chemical features of the
B. stearothermophilus
proteins which could explain the relative thermal stability of this organism's ribosomes.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
21 articles.
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