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. 1968 Feb;106(3):749–757. doi: 10.1042/bj1060749

The purification and amino acid composition of human uterus collagens, rheumatoid-arthritis-nodule collagen and ox tendon collagen

J J Harding 1,*, J M Wesley 1
PMCID: PMC1198568  PMID: 5639930

Abstract

Collagens and gelatins were isolated from human post-menopausal uterus, puerperal (post-partum) uterus, rheumatoid-arthritis-nodule and ox tendon. Different means of purifying collagen were studied and a method was devised that enables highly purified collagen to be obtained, even from the uterus. This method involves the use of a number of aqueous and organic extractants as well as digestion with elastase to eliminate elastin. The purity of the collagen preparations was assessed and they were used to study the amino acid composition of collagen. The amino acid compositions of all the collagens studied were similar to those of human bone and tendon collagen, but certain small differences were noted and are discussed. The soluble collagen extracted from some of the tissues was also studied.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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