The Amino Acid Sequence of Peptides from the Cross-Linking Region of Rat Skin Collagen

Andrew Kang, Paul Bornstein, Karl A. Piez

Research output: Contribution to journalArticle

95 Citations (Scopus)

Abstract

The amino acid sequences of two cyanogen bromide derived peptides from the cross-linking region at the NH2-terminal ends of the α1 and α2 chains of rat skin collagen have been established. The sequence of the pentadecapeptide from α1, α1-CB1, was found to be Gly-Tyr-Asp-Glu-Lys-Ser-Ala-Gly-Val-Ser-Val-Pro-Gly-Pro-Hse. The corresponding tetradecapeptide from α2, α2-CB1, was found to have the sequence PCA-Tyr-Ser-Asp-Lys-Gly-Val-Ser-Ala- Gly-Pro-Gly-Pro-Hse. These sequences are not typical of collagen and presumably cannot assume the helical configuration characteristic of the rest of the molecule. These findings may account for the selected susceptibility of the NH2-terminal region of native collagen to cleavage by a variety of proteolytic enzymes and by cyanogen bromide, and are consistent with the special role of this region as a site of cross-link formation through the lysyl side chains.

Original languageEnglish (US)
Pages (from-to)788-795
Number of pages8
JournalBiochemistry
Volume6
Issue number3
DOIs
StatePublished - Mar 1 1967
Externally publishedYes

Fingerprint

Rats
Amino Acid Sequence
Cyanogen Bromide
Skin
Collagen
Amino Acids
Peptides
Passive Cutaneous Anaphylaxis
Peptide Hydrolases
Molecules
poly(prolylprolylglycine)15

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

The Amino Acid Sequence of Peptides from the Cross-Linking Region of Rat Skin Collagen. / Kang, Andrew; Bornstein, Paul; Piez, Karl A.

In: Biochemistry, Vol. 6, No. 3, 01.03.1967, p. 788-795.

Research output: Contribution to journalArticle

Kang, Andrew ; Bornstein, Paul ; Piez, Karl A. / The Amino Acid Sequence of Peptides from the Cross-Linking Region of Rat Skin Collagen. In: Biochemistry. 1967 ; Vol. 6, No. 3. pp. 788-795.
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N2 - The amino acid sequences of two cyanogen bromide derived peptides from the cross-linking region at the NH2-terminal ends of the α1 and α2 chains of rat skin collagen have been established. The sequence of the pentadecapeptide from α1, α1-CB1, was found to be Gly-Tyr-Asp-Glu-Lys-Ser-Ala-Gly-Val-Ser-Val-Pro-Gly-Pro-Hse. The corresponding tetradecapeptide from α2, α2-CB1, was found to have the sequence PCA-Tyr-Ser-Asp-Lys-Gly-Val-Ser-Ala- Gly-Pro-Gly-Pro-Hse. These sequences are not typical of collagen and presumably cannot assume the helical configuration characteristic of the rest of the molecule. These findings may account for the selected susceptibility of the NH2-terminal region of native collagen to cleavage by a variety of proteolytic enzymes and by cyanogen bromide, and are consistent with the special role of this region as a site of cross-link formation through the lysyl side chains.

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