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Science 22 March 1974:
Vol. 183. no. 4130, pp. 1200 - 1201
DOI: 10.1126/science.183.4130.1200
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Articles

Collagen Polymorphism: Characterization of Molecules with the Chain Composition [agr1(III)]3 in Human Tissues

Endy Chung 1 and Edward J. Miller 2

1 Department of Pathology, Institute of Dental Research, University of Alabama Medical Center, Birmingham 35294
2 Department of Biochemistry, Institute of Dental Research, University of Alabama Medical Center

Collagen moleculess with the chain comizposition [agr1(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 ggr component (300,000 daltons). Reduction and alkylation of the high-molecular-weight component yields agr1(III) chains (95,000 daltons). In addition to containing cysteine, agr1(III) chains exhibit several other compositional differences when compared to agr1(I), agr1(II), or agr2 chains from human tissues.


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