title: Purification of salt-soluble cross-linked elastin by hydrophobic interaction chromatography.
abstract: The hydrophobic protein elastin, which is a major constituent of vascular and lung tissue is fragmented in several pathological conditions. The nature of the soluble fragments is not well understood. Such fragments bind to alkyl chains linked to agarose. Elution, which is effected by dimethylformamide and sodium dodecyl sulphate, is optimal from the decyl-agarose column. Dialysis of the eluates against buffered sodium chloride precipitates elastin, thus further purifying the salt-soluble cross-linked elastin.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002621:Chemistry; D002845:Chromatography / Q000379:methods; D004549:Elastin / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D011485:Protein Binding; D012492:Salts; D012756:Sheep; D012995:Solubility
chemical_list: D000596:Amino Acids; D012492:Salts; D004549:Elastin