Affiliation:
1. Pfizer Medical Research Laboratories, Chas. Pfizer & Co., Inc., Groton, Connecticut
Abstract
Day
, L. E. (Chas. Pfizer & Co., Inc., Groton, Conn.). Tetracycline inhibition of cell-free protein synthesis. I. Binding of tetracycline to components of the system. J. Bacteriol.
91:
1917–1923. 1966.—Tetracycline, an inhibitor of cell-free protein synthesis, effected the dissociation of
Escherichia coli
100
S
ribosomes to 70
S
particles in vivo and in vitro, but was not observed to mediate the further degradation of these particles. The antibiotic was bound by both 50
S
(Svedberg) and 30
S
subunits of 70
S
ribosomes and also by
E. coli
soluble RNA (sRNA), polyuridylic acid (poly U), and polyadenylic acid (poly A). The binding to ribosomal subunits was higher at 5 × 10
−4
m
Mg
++
than at 10
−2
m
Mg
++
. The binding to polynucleotide chains was highest when Mg
++
was not added to the reaction mixture.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
62 articles.
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