Polymorphism in human uterine collagen.

ABSTRACT

Fifty percent of human uterine collagen has been solubilized by limited pepsin digestion. Carboxymethyl cellulose-, Bio-gel A-5m-chromatography and amino acid analysis revealed that the solubilized collagen consists of 20% Type III and 80% Type I collagen. Reduction and alkylation reactions indicated that the alpha1(III) collagen is in the tissue as a trimer with the chain composition [alpha1(III)].