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Science 5 June 1964:
Vol. 144. no. 3623, pp. 1220 - 1221
DOI: 10.1126/science.144.3623.1220
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Articles

Intermolecular Cross-Linking of Collagen and the Identification of a New Beta-Component

Paul Bornstein 1, G. R. Martin 1, and Karl A. Piez 1

1 National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20014

Extraction of skin with 5M guanidine after salt and acid extraction yields a gelatin fraction which contains a greater proportion of double-chain (beta) components than can be accounted for by intramolecular cross-linking of collagen molecules. This fraction also contains a new beta-component, identified as the dimer of agr2 and designated beta22. This dimer must be formed by intermolecular crosslinking since each collagen molecule contains only one agr2 chain. Thus, direct evidence is presented for the occurrence of both inter- and intramolecular crosslinking by what appears to be a single continuous process.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Alterations in Collagen in the Arteries of Thromboangiitic Patients.
C. Peracchia and C. Vassallo (1966)
Angiology 17, 451-459
   PDF »
Beta-Components in Collagen.
S. Bakerman, P. Bornstein, G. R. Martin, and K. A. Piez (1964)
Science 145, 837
   PDF »


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