Rao C N, Margulies I M, Liotta L A
Biochem Biophys Res Commun. 1985 Apr 16;128(1):45-52. doi: 10.1016/0006-291x(85)91642-0.
Binding of type IV collagen to laminin was studied by attaching one member of the ligand pair to a solid phase. When laminin was bound to a solid phase, type IV collagen exhibited saturable binding. Digestion of type IV collagen with high concentrations of pepsin destroyed the laminin binding activity. Type IV collagen was also found to bind to fibronectin but the binding activity was not destroyed by pepsin treatment. Rotary shadowing electron microscopy of the pepsin digested type IV collagen indicated that the carboxy terminal end region of about 100 nm is cleaved. Rotary shadowing electron microscopy studies demonstrate that the carboxy terminal end of type IV collagen has a major laminin binding site.
通过将配体对中的一个成员附着到固相上来研究IV型胶原与层粘连蛋白的结合。当层粘连蛋白结合到固相上时，IV型胶原表现出饱和结合。用高浓度胃蛋白酶消化IV型胶原会破坏层粘连蛋白结合活性。还发现IV型胶原与纤连蛋白结合，但胃蛋白酶处理不会破坏结合活性。对经胃蛋白酶消化的IV型胶原进行旋转阴影电子显微镜观察表明，约100nm的羧基末端区域被切割。旋转阴影电子显微镜研究表明，IV型胶原的羧基末端有一个主要的层粘连蛋白结合位点。
