Isolation of a cross-linked dimer of elastin.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D003300:Copper / Q000172:deficiency; D004549:Elastin / Q000096:biosynthesis; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D013552:Swine
D000596:Amino Acids; D046911:Macromolecular Substances; D003300:Copper; D004549:Elastin