Covalent Structure of Collagen

Amino Acid Sequence of α2-CB5 of Chick Skin Collagen Containing the Animal Collagenase Cleavage Site

S. N. Dixit, C. L. Mainardi, J. M. Seyer, Andrew Kang

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

The amino acid sequence of the 112 residues from the amino terminus of α2-CB5 from chick skin collagen was determined by automated sequential degradation of intact α2-CB5 and several chymotryptic and tryptic peptides. This segment of the peptide includes the site of the action of animal collagenases. As compared to the sequence around the α1 cleavage site, the α2 sequence is notable for the remarkable constancy of the residues to the amino side and the relative abundance of hydrophobic residues to the carboxyl side of the cleavage site, suggesting that these features are important in the recognition by the enzyme. The sequence of this region of the α2 chain is consistent with the Gly-X-Y triplet structure and the preference of certain residues for either the X or Y position in distribution. However, three of the six residues of leucine were found in the Y position rather than the X position. Leucine residues were found only once in the Y position in the α 1(1) chain. This preference does not appear to hold in the αl chain.

Original languageEnglish (US)
Pages (from-to)5416-5422
Number of pages7
JournalBiochemistry
Volume18
Issue number24
DOIs
StatePublished - Jan 1 1979

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Collagenases
Leucine
Amino Acid Sequence
Skin
Animals
Collagen
Amino Acids
Peptides
Degradation
Enzymes

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Covalent Structure of Collagen : Amino Acid Sequence of α2-CB5 of Chick Skin Collagen Containing the Animal Collagenase Cleavage Site. / Dixit, S. N.; Mainardi, C. L.; Seyer, J. M.; Kang, Andrew.

In: Biochemistry, Vol. 18, No. 24, 01.01.1979, p. 5416-5422.

Research output: Contribution to journalArticle

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abstract = "The amino acid sequence of the 112 residues from the amino terminus of α2-CB5 from chick skin collagen was determined by automated sequential degradation of intact α2-CB5 and several chymotryptic and tryptic peptides. This segment of the peptide includes the site of the action of animal collagenases. As compared to the sequence around the α1 cleavage site, the α2 sequence is notable for the remarkable constancy of the residues to the amino side and the relative abundance of hydrophobic residues to the carboxyl side of the cleavage site, suggesting that these features are important in the recognition by the enzyme. The sequence of this region of the α2 chain is consistent with the Gly-X-Y triplet structure and the preference of certain residues for either the X or Y position in distribution. However, three of the six residues of leucine were found in the Y position rather than the X position. Leucine residues were found only once in the Y position in the α 1(1) chain. This preference does not appear to hold in the αl chain.",
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