The covalent structure of cartilage collagen. Evidence for sequence heterogeneity of bovine alpha1(II) chains
- PMID: 833147
The covalent structure of cartilage collagen. Evidence for sequence heterogeneity of bovine alpha1(II) chains
Abstract
During studies on the amino acid sequence of bovine nasal cartilage collagen, the cyanogen bromide peptide alpha1(II)-CB11 was degraded to smaller peptides with trypsin. One of the tryptic peptides, T5, which contained 39 residues was shown by amino acid and sequence analyses to occur in a predominant form that contained glutamine at position 5 and in a second form with leucine at this site. In addition to the heterogeneity at this position, amino acid analyses of five different preparations revealed that the peptide with leucine contained a seryl residue not found in the major form. Sequence heterogeneity at a third position of alpha1(II) was demonstrated by the isolation of a hexapeptide (T2) from the trypsin digest of alpha1(II)-CB11 which contained 0.21 residue of alanine and 0.77 of leucine. Both the leucine and alanine of T2 were removed after the second cycle of subtractive Edman degradation. These data show that at least two types of alpha1(II) chains, designated as alpha1(II)Major and alpha1(II)Minor, exist in bovine nasal cartilage. Further considerations suggest that these two chains are probably not variants derived from allelic genes but are the products of separate genes.
Similar articles
-
The covalent structure of cartilage collagen. Amino acid sequence of residues 552-661 of bovine alpha1(II) chains.Biochem J. 1978 Dec 1;175(3):921-30. doi: 10.1042/bj1750921. Biochem J. 1978. PMID: 743239 Free PMC article.
-
The covalent structure of collagen: amino-acid sequence of the cyanogen-bromide peptides alpha1-CB2, alpha1-CB4 and alpha1-CB5 from calf-skin collagen.Eur J Biochem. 1975 Mar 3;52(1):77-82. doi: 10.1111/j.1432-1033.1975.tb03974.x. Eur J Biochem. 1975. PMID: 1164916
-
Covalent structure of collagen. Amino acid sequence of an arthritogenic cyanogen bromide peptide from type II collagen of bovine cartilage.Eur J Biochem. 1989 Apr 15;181(1):159-73. doi: 10.1111/j.1432-1033.1989.tb14707.x. Eur J Biochem. 1989. PMID: 2714276
-
Covalent structure of collagen: amino acid sequence of cyanogen bromide peptides from the amino-terminal segment of type III collagen of human liver.Biochemistry. 1977 Mar 22;16(6):1158-64. doi: 10.1021/bi00625a020. Biochemistry. 1977. PMID: 557335
-
Covalent structure of collagen: amino acid sequence of alpha1-CB6A of chick skin collagen.Biochemistry. 1975 May 6;14(9):1933-8. doi: 10.1021/bi00680a020. Biochemistry. 1975. PMID: 1125204
Cited by
-
LC-MS/MS identification of the O-glycosylation and hydroxylation of amino acid residues of collagen α-1 (II) chain from bovine cartilage.J Proteome Res. 2013 Aug 2;12(8):3599-609. doi: 10.1021/pr400101t. Epub 2013 Jul 23. J Proteome Res. 2013. PMID: 23879958 Free PMC article.
-
Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule.Biochem J. 1983 Oct 1;215(1):175-82. doi: 10.1042/bj2150175. Biochem J. 1983. PMID: 6626173 Free PMC article.
-
Isolation and partial characterization of proteoglycans from rat incisors.Biochem J. 1984 Mar 15;218(3):877-85. doi: 10.1042/bj2180877. Biochem J. 1984. PMID: 6721839 Free PMC article.
-
Mucosal tolerance and suppression of collagen-induced arthritis (CIA) induced by nasal inhalation of synthetic peptide 184-198 of bovine type II collagen (CII) expressing a dominant T cell epitope.Clin Exp Immunol. 1996 Mar;103(3):368-75. doi: 10.1111/j.1365-2249.1996.tb08289.x. Clin Exp Immunol. 1996. PMID: 8608633 Free PMC article.
-
The covalent structure of cartilage collagen. Amino acid sequence of residues 552-661 of bovine alpha1(II) chains.Biochem J. 1978 Dec 1;175(3):921-30. doi: 10.1042/bj1750921. Biochem J. 1978. PMID: 743239 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
