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

1979; Elsevier BV; Volume: 254; Issue: 5 Linguagem: Inglês

10.1016/s0021-9258(17)37782-7

1083-351X

G. Balian, E M Click, Ed Crouch, Jeffrey M. Davidson, Paul Börnstein,

Glycosylation and Glycoproteins Research

Limited proteolytic cleavage of fibronectin and plasma cold-insoluble globulin with cathepsin D produced two major fragments.The smaller, M, = 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 twothirds of the linear distance from the NH2 terminus of each chain in the dimeric molecule.