Document Detail

The structure of a small collagenous fragment isolated from chicken hyaline cartilage.
MedLine Citation:
PMID:  3988818     Owner:  NLM     Status:  MEDLINE    
In previous experiments, two collagenous fragments were isolated from pepsin digests of chicken hyaline cartilage and called the high molecular weight, (HMW) and low molecular weight (LMW) fractions [3]. In the present experiments, the chains of LMW were isolated after denaturation and subsequent reduction and alkylation of interchain disulfide bridges and were further fractionated by carboxymethyl-cellulose chromatography. Four peaks were resolved during chromatography and were designated LMW 1, 2A, 2B, and 3. Amino acid analyses and peptide mapping after cleavage with trypsin, V8 protease, and cyanogen bromide showed that three genetically distinct chains must be present in LMW. Fractions 2A and 2B were very similar, but not identical, in structure. LMW 1, 2A plus 2B, and 3 were consistently isolated in approximately equal proportions, suggesting that the probable chain organization of LMW is [1][2A + 2B][3]. This suggestion was supported further by experiments that attempted to fractionate LMW by carboxymethyl-cellulose chromatography after denaturation but without reduction and alkylation of interchain disulfide bridges. No fractionation of LMW was achieved, the single peak subsequently being shown to contain LMW 1, 2A plus 2B, and 3.
R Mayne; M van der Rest; D C Weaver; W T Butler
Related Documents :
7346218 - Two-dimensional cnbr peptide patterns of collagen types i, ii and iii.
791788 - Isolation and characterization of cnbr derived peptides of the alpha1 (iii) chain of pe...
8486658 - Use of endoproteases to identify catalytic domains, linker regions, and functional inte...
9724608 - Gly-x-y tripeptide frequencies in collagen: a context for host-guest triple-helical pep...
15446238 - Grafting rgd containing peptides onto hydroxyapatite to promote osteoblastic cells adhe...
24279498 - Engineering antimicrobial peptides with improved antimicrobial and hemolytic activities.
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of cellular biochemistry     Volume:  27     ISSN:  0730-2312     ISO Abbreviation:  J. Cell. Biochem.     Publication Date:  1985  
Date Detail:
Created Date:  1985-06-06     Completed Date:  1985-06-06     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8205768     Medline TA:  J Cell Biochem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  133-41     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Cartilage / analysis*
Collagen / isolation & purification*
Molecular Weight
Peptide Fragments / isolation & purification
Protein Conformation
Grant Support
Reg. No./Substance:
0/Peptide Fragments; 9007-34-5/Collagen

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

Previous Document:  Metabolic properties of an azaguanine-resistant variant of Chinese hamster ovary cells (azarts) with...
Next Document:  Comparisons of evolutionarily distinct fibronectins: evidence for the origin of plasma and fibroblas...