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PMID: 4958942 Published · ppublish English Journal Article

Cell-free protein synthesis: effects of age and state of ribosomal aggregation.

Science (New York, N.Y.) ·Vol. 154 ·No. 3754 ·1966-12-09 ·Pages 1350-3

Moore LD, Kocun FJ, Umbreit WW

Abstract

In cell-free extracts derived from Streptococcus faecalis, protein synthesis directed by endogenous messenger RNA increases as the culture ages. The increased activity is accompanied by an increase in the percentage of membranebound ribosomes and by a decrease in ribosomal monomers and subunits. These changes progress against a background of structural and compositional modifications in the membrane. Membrane modifications possibly related to endogenously directed protein synthesis in cell-free extracts include: (i) decreased specific activity of a membrane-associated polynucleotide phosphorylase capable of polysome degradation, and (ii) increased concentrations of certain phospholipids.

MeSH Terms
Culture Techniques Enterococcus faecalis Nucleotidyltransferases/analysis Phospholipids Phosphorus Isotopes Protein Biosynthesis RNA, Messenger/physiology Ribosomes
Chemicals
Phospholipids Phosphorus Isotopes RNA, Messenger Nucleotidyltransferases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Moore L D
Kocun F J
Umbreit W W
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1966-12-09
Pages
1350-3
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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