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 language | English |
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Pages (from-to) | 1429-1432 |
Number of pages | 4 |
Journal | Journal of Biological Chemistry |
Volume | 254 |
Issue number | 5 |
State | Published - 1979 |