Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin.
Limited proteolytic cleavage of fibronectin and plasma cold-insoluble globulin with cathepsin D produced two major fragments. The smaller, Mr = 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 NH2 terminus of each chain in the dimeric molecule.
D000596:Amino Acids / Q000032:analysis; D000653:Amniotic Fluid; D002403:Cathepsins; D002478:Cells, Cultured; D003080:Cold Temperature; D003094:Collagen; D004220:Disulfides; D005260:Female; D005916:Globulins; D006023:Glycoproteins; D006801:Humans; D046911:Macromolecular Substances; D008565:Membrane Proteins; D008970:Molecular Weight; D011247:Pregnancy; D011485:Protein Binding
D000596:Amino Acids; D004220:Disulfides; D005916:Globulins; D006023:Glycoproteins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D003094:Collagen; D002403:Cathepsins