Abstract
The total yield of salt-soluble and acetic acid-soluble collagens of human uterus, prepared in purified states, is approximately 0.06% by wet weight of tissue. After heat denaturation, the β- and α-components were separated on Sephadex G-200 columns. The separation of β 11 and β 12 and α 1 and α 2 was accomplished on carboxymethyl cellulose columns. The amino acid composition of each component, so separated, was determined. In comparison with salt-soluble collagen of skin, uterine salt-soluble collagen contains less α-component and more β-component. Amino acid analysis revealed that uterine collagen contained a somewhat higher level of hydroxyproline and hydroxylysine than dermal collagen. Cysteic acid, not seen in collagen from other mammalian tissues, was consistently present in all preparations at levels approximating 1 residue/1000 residues.
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