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- W1513455608 abstract "Salt-soluble elastin, isolated by coacervation from extracts of copper-deficient pig aorta, contains a minor protein component separable by gel electrophoresis in 6 M urea. This protein has a molecular weight of 150,000 compared to 75,000 of the major component. The amino acid analyses of both proteins are typical of elastin but the higher molecular weight component has a significantly lower lysine content and lysine-derived cross-links that are lacking from the major component. The proteins were labeled by incubation of the fresh aortic tissue with [14C]lysine. The acid hydrolysate of the borohydride-reduced higher molecular weight protein contained a labeled amino acid eluting at a time identical to standard merodesmosine and a trace of radioactivity corresponding to lysinonorleucine. We conclude that the higher molecular weight protein is a cross-linked dimer of the previously identified soluble elastin." @default.
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- W1513455608 date "1978-11-01" @default.
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- W1513455608 title "Isolation of a cross-linked dimer of elastin." @default.
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- W1513455608 doi "https://doi.org/10.1016/s0021-9258(17)34347-8" @default.
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