Identification of the loci of the collagen-associated Ehrlich chromogen in type I collagen confirms its role as a trivalent cross-link
| Autor: | M Tyler, Ian D. Jenkins, Ronald Kuypers, Douglas J. Horgan, Lyndon B. Kurth |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1992 |
| Předmět: |
Stereochemistry
Molecular Sequence Data Biochemistry Aldehyde chemistry.chemical_compound Animals Trypsin Amino Acid Sequence Bifunctional Molecular Biology Chromatography High Pressure Liquid Pyrrole chemistry.chemical_classification Pyridinoline integumentary system Cross-link Cell Biology Amino acid Molecular Weight Cross-Linking Reagents chemistry Chromogenic Compounds Cattle Collagen Glycoprotein Peptides Azo Compounds Type I collagen Research Article |
| Popis: | Collagenous peptides containing the Ehrlich chromogen (EC) were selectively isolated from a tryptic digest of bovine tendon by coupling to a diazotized polyacrylamide support. The isolated p-phenol-azo-EC peptides were purified and characterized by amino acid and sequence analyses. EC occurred in stoichiometric amounts in trimeric cross-linked chains originating from the known cross-link regions of type-I collagen. The major locus of the EC was alpha 2(I)Hyl-933 x alpha 1(I)Lys(Hyl)-9N x alpha 2(I)Lys(Hyl)-5N but it was also shown to occur at the loci alpha 1(I)Hyl-87 x alpha 1(I)Lys(Hyl)-16C x alpha 1(I)Lys(Hyl)-16C and alpha 1(I)Hyl-930 x alpha 1(I)Lys(Hyl)-9N x alpha 2(I)Lys(Hyl)-5N. After sequence analyses of the C-terminal helical cross-link region alpha 2(I)928-963, corrections are presented for residues 927, 930, 932 and 933 of the bovine alpha 2(I) chain. The collagen-associated EC is postulated to be a trisubstituted pyrrole formed by the reaction of the aldehyde form of a telopeptidyl lysine residue with a bifunctional keto amino cross-link. It is also proposed that when the telopeptidyl lysine residue is hydroxylated the above reaction will result in pyridinoline formation. |
| Databáze: | OpenAIRE |
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