Document Detail


Fractionation of pepsin-digested, denatured collagen. III. Characterization of the small fragments.
MedLine Citation:
PMID:  11452378     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The survey of the fragments obtained from pepsin-digested, denatured rat tail tendon collagen is completed. Three additional fragments could be renatured and two of them (490 A and 670 A) were located in tropocollagen by electron microscopy. Data are given on the amino acid compositions of the various fractions. Certain fragments probably originated from the associated non-collagenous material belonging to the "acidic structural proteins".
Authors:
J Pikkarainen; K Lampiaho; E Kulonen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  251     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1971 Nov 
Date Detail:
Created Date:  2001-07-16     Completed Date:  2001-08-02     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  141-8     Citation Subset:  IM    
Affiliation:
Department of Medical Chemistry, University of Turku, Turku 52, Finland.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Animals
Collagen / chemistry,  ultrastructure*
Microscopy, Electron
Pepsin A*
Peptide Fragments / chemistry,  ultrastructure
Protein Denaturation
Rats
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Peptide Fragments; 9007-34-5/Collagen; EC 3.4.23.1/Pepsin A

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


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