Collagen Polymorphism: Characterization of Molecules with the Chain Composition [α1(III)] 3 in Human Tissues

Abstract

Collagen moleculess with the chain comizposition [α1(III)]₃, have been isolated from pepsin-solubilized collagen of dermis, aorta, and leiomlyoma of the uterus by differential salt precipitation. On denaturation, approximately 90 percent of this collagen is recovered as a γ component (300,000 daltons). Reduction and alkylation of the high-molecular-weight component yields α1(III) chains (95,000 daltons). In addition to containing cysteine, α1(III) chains exhibit several other compositional differences when compared to α1(I), α1(II), or α2 chains from human tissues.