Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin

G. Balian, E. M. Click, E. Crouch, J. M. Davidson, P. Bornstein

Research output: Contribution to journalArticlepeer-review

142 Scopus citations

Abstract

Limited proteolytic cleavage of fibronectin and plasma cold-insoluble globulin with cathepsin D produced two major fragments. The smaller, M(r) = 72,000 fragment bound to collagen and contained most of the cysteine in the molecule. This region contains intrachain disulfide bonds which maintain a conformation that is necessary for interaction with collagen. Cleavage of the intact protein and the 72,000-dalton fragment with plasmin localized the collagen-binding region in cold-insoluble globulin to a sequence of about 42,000 daltons. This region is located approximately two-thirds of the linear distance from the NH 2 terminus of each chain in the dimeric molecule.

Original languageEnglish
Pages (from-to)1429-1432
Number of pages4
JournalJournal of Biological Chemistry
Volume254
Issue number5
StatePublished - 1979

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