An 'Affinity' Method for Preparing Polypeptides Enriched in the Collagen-Associated Ehrlich Chromogen
- 1 March 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 93 (3) , 921-925
- https://doi.org/10.1093/jb/93.3.921
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.Keywords
This publication has 5 references indexed in Scilit:
- An Ehrlich chromogen in collagen cross-linksBiochemical Journal, 1983
- A collagen-associated Ehrlich chromogen: a pyrrolic cross-link?Bioscience Reports, 1981
- Location of an Intermolecular Crosslink in Bovine Bone CollagenConnective Tissue Research, 1981
- Isolation of Crosslinked Peptides from Insoluble Human LeiomyomaEuropean Journal of Biochemistry, 1979
- The structure of pyridinoline, a collagen crosslinkBiochemical and Biophysical Research Communications, 1978