Collagen-induced platelet aggregation: Involvement of an active glycopeptide fragment (α1-CB5)

Richard L. Katzman, Andrew Kang, Edwin H. Beachey

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

It is widely held that the tertiary structure of collagen is essential for induction of platelet aggregation. However, we have found that the purified α1 chain prepared from denatured chick skin collagen aggregates platelets. This activity appears to be confined to a distinct region of the molecule representing less than 4 percent of the length of the α1 chain. Of all of the cyanogen bromide peptides of the al chain tested, only one (α1-CB5) was active. This glycopeptide, devoid of any ordered tertiary structure, contains only 36 amino acids and one residue of O-α-O-glucopyranosyl-(1 → 2)-O-β-D-galactopyranosyloxy-(1 → 5)-lysine (Glc-Gal-Hyl). Blocking experiments strongly suggest that the Glc-Gal-Hyl is one of the structural determinants involved in collagen-induced platelet aggregation.

Original languageEnglish (US)
Pages (from-to)670-672
Number of pages3
JournalScience
Volume181
Issue number4100
DOIs
StatePublished - Jan 1 1973

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Glycopeptides
Platelet Aggregation
Collagen
Cyanogen Bromide
Lysine
Blood Platelets
Amino Acids
Skin
Peptides
hydroxylysine glycoside

All Science Journal Classification (ASJC) codes

  • General

Cite this

Collagen-induced platelet aggregation : Involvement of an active glycopeptide fragment (α1-CB5). / Katzman, Richard L.; Kang, Andrew; Beachey, Edwin H.

In: Science, Vol. 181, No. 4100, 01.01.1973, p. 670-672.

Research output: Contribution to journalArticle

Katzman, Richard L. ; Kang, Andrew ; Beachey, Edwin H. / Collagen-induced platelet aggregation : Involvement of an active glycopeptide fragment (α1-CB5). In: Science. 1973 ; Vol. 181, No. 4100. pp. 670-672.
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