Binding of prostaglandin to human serum albumin.
作者： W. G. UNGER
DOI: 10.1111/J.2042-7158.1972.TB09034.X
关键词:
摘要: Equilibrium dialysis and incubation experiments were used to examine the interaction of prostaglandin E1 (3H-PGE1) with various constituents human blood. Prostaglandins bound serum albumin more weakly than saturated other unsaturated fatty acids chain lengths. Blood cells plasma globulins did not interact PG. When proteins precipitated by ethanol as a preliminary stage extracting PG from recoveries added PGs poor. The addition acid non-precipitating amounts (40-50%) permitted quantitative extraction PGE F A compounds into chloroform. These results do allow definition physicochemical nature PG/albumin association certainty. However primary binding energy is most likely hydrophobic; or methanol reduced both constant molar ratio albumin.
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