Literature DB >> 6874673

An 'affinity' method for preparing polypeptides enriched in the collagen-associated Ehrlich chromogen.

J E Scott, E W Hughes, A Shuttleworth.   

Abstract

The collagen-associated compound which reacts at room temperature with acid dimethylaminobenzaldehyde (Ehrlichs reagent) also reacts in acid with aryl-diazonium reagents. We have developed a convenient method for isolating polypeptides associated with the Ehrlich chromogen from collagen digests utilizing diazotized arylamino-cellulose supports. These peptides, in which the Ehrlich chromogen is 'labeled' with yellow diazo color, constitute less than 0.5% of the collagen, and have amino acid patterns similar to those around the cross link regions. The chromogen is not identical with pyridinoline, also thought to be a polyvalent cross link.

Entities:  

Mesh:

Substances:

Year:  1983        PMID: 6874673     DOI: 10.1093/jb/93.3.921

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  3 in total

1.  Glycosylation and cross-linking in bone type I collagen.

Authors:  Masahiko Terajima; Irina Perdivara; Marnisa Sricholpech; Yoshizumi Deguchi; Nancy Pleshko; Kenneth B Tomer; Mitsuo Yamauchi
Journal:  J Biol Chem       Date:  2014-06-23       Impact factor: 5.157

2.  Identification of the loci of the collagen-associated Ehrlich chromogen in type I collagen confirms its role as a trivalent cross-link.

Authors:  R Kuypers; M Tyler; L B Kurth; I D Jenkins; D J Horgan
Journal:  Biochem J       Date:  1992-04-01       Impact factor: 3.857

3.  Ehrlich chromogens, probable cross-links in elastin and collagen.

Authors:  P D Kemp; J E Scott
Journal:  Biochem J       Date:  1988-06-01       Impact factor: 3.857

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.