Open AccessCovalent structure of collagen
Author(s) -
SEYER Jerome M.,
HASTY Karen A.,
KANG Andrew H.
Publication year - 1989
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1989.tb14707.x
Subject(s) - cyanogen bromide , thermolysin , trypsin , chemistry , edman degradation , sephadex , size exclusion chromatography , peptide , peptide sequence , amino acid , chymotrypsin , pepsin , chromatography , gel permeation chromatography , papain , type ii collagen , biochemistry , cartilage , enzyme , biology , organic chemistry , anatomy , gene , polymer
Bovine articular type II collagen was prepared by limited pepsin digestion, differential salt fractionation and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type II collagen α chains yielded twelve distinct peptides designated CB1–12. The peptide α1(II)‐CB11 was isolated by carboxymethylcellulose chromatography and Sephadex G‐75S gel filtration. Automated Edman degradation together with chymotrypsin, thermolysin and trypsin digestion enabled identification of its complete amino acid sequence. Compared with type I and type III collagen, the data show similarity with α1(I)‐CB8 and α1(III)‐CB6‐1‐8‐10‐2 peptides, respectively. The peptide is located within residues 124–402 of the α1(II) collagen chain and with its identification, now extends the known amino acid sequence of bovine type II cartilage collagen to 660 amino acid residues including α1(II)‐CB1‐2‐6‐12‐11‐8‐10 (partial). This corresponds to α1(I)‐CB0‐1‐2‐4‐5‐8‐3‐7 (partial; 1–660) and α1(III)‐CB3A‐3B‐3C‐7‐6‐1‐8‐10‐2‐4‐5 (partial; 1–660) of bovine α1(I) and α1(III) collagen chains.