title: Type-IV collagens. Isolation and characterization of two structurally distinct collagen chains from bovine kidney cortices.
abstract: Two sets of structurally distinct collagen components resembling type IV collagen have been isolated and purified from the pepsin digest of kidney cortex homogenates. C and D chains with the size of alpha chains were separated from disulfide-linked material on molecular sieves and were further purified by ion-exchange chromatography. The molecular gel filtration of the starting material also gave two high-molecular-weight collageneous fractions. The reduction of these fractions with dithiothreitol followed by carboxymethyl-cellulose chromatography resulted in the separation of two major peaks, one corresponding to C-1 and the second peak corresponding to D-1 and a 75 000-Mr components. These latter two components were further separated from each other by molecular sieve chromatography. In addition some smaller peptides (two 50 000-Mr and one 15 000-Mr peptides) were purified and analkyzed. By amino acid composition, chromatographic properties and cyanogen bromide peptide patterns on sodium dodecyl sulfate/polyacrylamide gel electrophoresis, the C-1 and C chains and one of the 50 000-Mr components appear to be derived from the same chain by pepsin cleavage at different sites. Similarly, the D1 and D chains, and the 75 000-Mr, the second 50 000-Mr and the 15 000-Mr components are related to each other but are structurally distinct from the C-1 and C components. The presented data are consistent with the presence of two structurally distinct chains in basement membrane collageneous molecules.
mesh_terms: D000478:Alkylation; D000818:Animals; D002417:Cattle; D002845:Chromatography; D003094:Collagen / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D007672:Kidney Cortex / Q000032:analysis*; D008970:Molecular Weight; D010084:Oxidation-Reduction
chemical_list: D003094:Collagen