Covalent Structure of Collagen

Isolation of Chymotryptic Peptides and Amino Acid Sequence of the Amino‐Terminal Region of α2‐CB3 from Chick Skin

Saryu N. DIXIT, Jerome M. SEYER, Andrew Kang

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Five chymotryptic peptides were isolated from α2‐CB3 of chick skin collagen by a combination of ion‐exchange and molecular sieve chromatography. Together, they account for the entire amino acid content of the parent peptide. Their alignment was deduced by isolation and sequence analyses of overlapping tryptic peptides. In addition, the amino acid sequence of the three consecutive chymotryptic peptides, containing 132 amino acid residues, from the NH2‐terminus of α2‐CB3 was determined by automated Edman degradation of the peptides and tryptic peptides derived from them. The resulting sequence shows an identity of approximately 80% when compared with those of the homologous portions of rat and calf skin collagen. In contrast, extensive substitutions are present when the sequence was compared with that of the corresponding segment of the α1 chain from the same species.

Original languageEnglish (US)
Pages (from-to)213-221
Number of pages9
JournalEuropean Journal of Biochemistry
Volume73
Issue number1
DOIs
StatePublished - Jan 1 1977
Externally publishedYes

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Amino Acid Sequence
Skin
Collagen
Amino Acids
Peptides
Molecular sieves
Chromatography
Gel Chromatography
Sequence Analysis
Rats
Substitution reactions
Degradation

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Covalent Structure of Collagen : Isolation of Chymotryptic Peptides and Amino Acid Sequence of the Amino‐Terminal Region of α2‐CB3 from Chick Skin. / DIXIT, Saryu N.; SEYER, Jerome M.; Kang, Andrew.

In: European Journal of Biochemistry, Vol. 73, No. 1, 01.01.1977, p. 213-221.

Research output: Contribution to journalArticle

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