Separation and characterization of two polypeptide chains from the 7S cross-linking domain of basement-membrane (type IV) collagen

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Abstract
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 2 polypeptide chains of MW about 25,000. Compositional data and CNBr peptide patterns showed that the 2 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.