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PMID: 4347780 Published · ppublish English Journal Article

Binding of rat liver and hepatoma polyribosomes to stripped rough endoplasmic reticulum in vitro. Biological or an artifact?

The Biochemical journal ·Vol. 130 ·No. 1 ·1972-11-00 ·Pages 19-25

Hochberg AA, Stratman FW, Zahlten RN, Morris HP, Lardy HA

Abstract

Exposed thiol groups do not appear to be related to the binding of (32)P-labelled polyribosomes to stripped rough endoplasmic reticulum in vitro. Treating stripped rough endoplasmic reticulum with GSSG did not diminish binding of polyribosomes, suggesting that binding in vitro has no correlation with the inhibition of protein synthesis in vitro reported by Kosower et al. (1971). Thiol reagents, which are known to dissociate ribosomes, did not significantly decrease binding of (32)P-labelled polyribosomes to stripped rough endoplasmic reticulum. Denaturing the protein of (32)P-labelled polyribosomes or stripped rough endoplasmic reticulum of liver or hepatoma with heat, trichloroacetic acid, or HClO(4) did not alter the binding in vitro. Therefore, the practice of measuring the binding of (32)P-labelled polyribosomes to stripped rough endoplasmic reticulum in vitro (Shires et al., 1971b) is an unsuitable indicator of biological significance in the intact cell.

MeSH Terms
Animals Binding Sites Carcinoma, Hepatocellular Centrifugation, Density Gradient Endoplasmic Reticulum Female In Vitro Techniques Liver Liver Neoplasms Phosphorus Isotopes Polyribosomes Protein Denaturation Proteins/analysis Rats Sulfhydryl Compounds Temperature Trichloroacetic Acid
Chemicals
Phosphorus Isotopes Proteins Sulfhydryl Compounds Trichloroacetic Acid
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Hochberg A A
Stratman F W
Zahlten R N
Morris H P
Lardy H A
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26 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1300019
Published
1972-11-00
Pages
19-25
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1174296
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1300019 PMC Full Text View journal details
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