Comparative Studies on the Amino Acid Sequence of the α2-CB2 Peptides from Chick and Rat Skin Collagens

John H. Highberger, Andrew Kang, Jerome Gross

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

The amino acid sequence of the 30-residue cyanogen bromide peptide (α2-CB2) from the α2 chain of chick skin collagen has been determined by the Edman degradation-dansylation method applied to its tryptic digestion products. Confirmation of the structure was obtained by study of additional overlapping peptides isolated from a thermolytic digest. The primary structure consists of the triplet sequence generally characteristic of collagen, with glycine every third residue, and hydroxyproline occurring only in position 3. The sequence of the NH2-terminal-half of the homologous peptide from rat skin collagen has also been determined. This portion of the molecule contains all of the three substitutions between the two species found in these peptides. In contrast to the well-known resistance of the arginyl-proline bond, the arginyl-hydroxyproline bond in α2-CB2 was found to be slowly cleaved by trypsin in Tris buffer at pH 7.5.

Original languageEnglish (US)
Pages (from-to)610-616
Number of pages7
JournalBiochemistry
Volume10
Issue number4
DOIs
StatePublished - Feb 1 1971
Externally publishedYes

Fingerprint

Rats
Amino Acid Sequence
Skin
Collagen
Amino Acids
Peptides
Hydroxyproline
Cyanogen Bromide
Tromethamine
Proline
Glycine
Trypsin
Digestion
Substitution reactions
Degradation
Molecules

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Comparative Studies on the Amino Acid Sequence of the α2-CB2 Peptides from Chick and Rat Skin Collagens. / Highberger, John H.; Kang, Andrew; Gross, Jerome.

In: Biochemistry, Vol. 10, No. 4, 01.02.1971, p. 610-616.

Research output: Contribution to journalArticle

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