Document Detail

Biochemical characterization of the cuticle collagen of the nematode Caenorhabditis elegans.
MedLine Citation:
PMID:  7284437     Owner:  NLM     Status:  MEDLINE    
Proteins of purified cuticles from adults of the small free-living nematode Caenorhabditis elegans are solubilized by reduction in the presence of a strong denaturing agent and then carboxymethylated. As in the large parasitic nematode Ascaris lumbricoïdes, these soluble proteins appeared to be collagens by their amino acid compositions. C. elegans cuticle collagen is separated into seven major components with different apparent molecular weights by molecular sieve chromatography and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The two main components, which together account for more than 64% of the total cuticle collagen, were extracted from gel after electrophoresis and analyzed. They differ in their amino acid compositions and would seem to represent genetically distinct collagen chains. The results presented lead to the hypothesis of the presence in this collagen of at least two different chains.
R Ouazana; D Herbage
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  669     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1981 Jul 
Date Detail:
Created Date:  1981-12-15     Completed Date:  1981-12-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  236-43     Citation Subset:  IM    
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MeSH Terms
Amino Acids / analysis
Caenorhabditis / analysis*,  ultrastructure
Chromatography, Gel
Collagen / isolation & purification*
Microscopy, Electron
Molecular Weight
Proteins / isolation & purification
Reg. No./Substance:
0/Amino Acids; 0/Proteins; 9007-34-5/Collagen

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