Separation and characterization of two polypeptide chains from the 7S cross-linking domain of basement-membrane (type IV) collagen.
The long-form 7S domain of human placental type IV collagen was prepared and after reduction, denaturation and aminoethylation, was separated into its subunits. The monomer subunit was further separated into two polypeptide chains of Mr about 25 000. From compositional data and CNBr peptide patterns it was shown that the two chains were different. Furthermore, all subunits contained both chains, thus supporting a proposed subunit structure for the 7S domain and a chain composition [alpha 1(IV)]2 alpha 2(IV) for the type IV molecule.
D000596:Amino Acids / Q000032:analysis; D001485:Basement Membrane / Q000032:analysis; D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D003094:Collagen; D003488:Cyanogen Bromide; D006801:Humans; D003012:Microbial Collagenase; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis*; D011487:Protein Conformation
D000596:Amino Acids; D010446:Peptide Fragments; D003094:Collagen; D003012:Microbial Collagenase; D003488:Cyanogen Bromide