Document Detail


Sulfhydryl group quantitation of hepatoma and liver microsomal fractions.
MedLine Citation:
PMID:  165877     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The relationship of sulfhydryl and disulfide groups to protein synthesis in normal and rapidly growing tissues was investigated by quantitation of sulfhydryl groups in endoplasmic reticulum and polyribosomes of normal liver and hepatomas. Stripping by ethylenediaminetetraacetate and potassium chloride of normal liver smooth and rough endoplasmic reticulum reduced by 15 percent and increased 30 percent, respectively, the sulfhydryl groups available for carboxamidemethylation by iodoacetamide. This could reflect the removal of ribosomes from rough endoplasmic reticulum with the subsequent exposure of sulfhydryl groups. Exposed sulfhydryl groups of normal mature female rat liver smooth endoplasmic reticulum were decreased to a similar degree by the stripping procedure with ethylenediaminetetra-acetate and potassium chloride when quantitated by either iodoacetamide or 4,4'-dithiodipyridine. This was not the case in young male and female rats, where the stripping procedure failed to decrease the exposed sulfhydryl groups of smooth endoplasmic reticulum. An increase in the quantity of exposed sulfhydryl groups of normal young and mature rat liver rough endoplasmic reticulum after stripping by ethylenediaminetetraacetate and potassium chloride was observed with iodoacetamide. However, when 4,4'-dithiodipyridine was used, no change could be detected. The hypothesis that smooth endoplasmic reticulum arises by degranulation of the rough endoplasmic reticulum in vivo is not supported by our sulfhydryl group quantitation of smooth endoplasmic reticulum and in vitro degranulated rough endoplasmic reticulum. A negative correlation between exposed sulfhydryl groups on the polyribosomes and the rate of growth of normal liver and of Morris hepatomas 6 and 38B suggests that the conformation of the free polyribosomal proteins could be a control factor for the rate of protein synthesis. Faster growing hepatomas also have greater quantities of sulfhydryls and disulfides.
Authors:
F W Stratman; A A Hochberg; R N Zahlten; H P Morris
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Cancer research     Volume:  35     ISSN:  0008-5472     ISO Abbreviation:  Cancer Res.     Publication Date:  1975 Jun 
Date Detail:
Created Date:  1975-09-04     Completed Date:  1975-09-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2984705R     Medline TA:  Cancer Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1476-84     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Age Factors
Animals
Carcinoma, Hepatocellular / metabolism*
Cell Fractionation
Disulfides / metabolism
Edetic Acid
Endoplasmic Reticulum / metabolism
Female
Iodamide
Liver / ultrastructure
Liver Neoplasms / metabolism*
Male
Methylation
Microsomes, Liver / metabolism*
Neoplasms, Experimental / metabolism
Polyribosomes / metabolism
Potassium Chloride
Protein Binding
Protein Conformation
Pyridines
Rats
Sex Factors
Sulfhydryl Compounds / analysis*
Sulfhydryl Reagents
Urea
Chemical
Reg. No./Substance:
0/Disulfides; 0/Pyridines; 0/Sulfhydryl Compounds; 0/Sulfhydryl Reagents; 440-58-4/Iodamide; 57-13-6/Urea; 60-00-4/Edetic Acid; 7447-40-7/Potassium Chloride

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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