Isolation and Characterization of CrossLinked Peptides from Elastin

Two peptides containing the desmosine cross-link were isolated and purified from a subtilisin digest of oxalic acidsolubilized elastin. Molecular weights averaged approximately 6000. Automated sequence data suggest that the desmosines cross-link two polypeptide chains and that both desmosine and iso...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 249; no. 19; pp. 6191 - 6196
Main Authors:	Foster, Judith Ann, Rubin, Lisa, Kagan, Herbert M., Franzblau, Carl, Bruenger, Eveline, Sandberg, Lawrence B.
Format:	Journal Article
Language:	English
Published:	Elsevier Inc 10-10-1974 American Society for Biochemistry and Molecular Biology
Online Access:	Get full text
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Summary:	Two peptides containing the desmosine cross-link were isolated and purified from a subtilisin digest of oxalic acidsolubilized elastin. Molecular weights averaged approximately 6000. Automated sequence data suggest that the desmosines cross-link two polypeptide chains and that both desmosine and isodesmosine are present in the same primary sequence approximately equally substituted. The primary sequence of the peptides is in good agreement with sequence data obtained on the soluble elastin precursor tropoelastin.
ISSN:	0021-9258 1083-351X
DOI:	10.1016/S0021-9258(19)42239-4