Purification and properties of human serum esterase.
Human serum esterase was purified by affinity column chromatography on a column of covalently linked p-trimethylammoniumanilinium dichloride to Sepharose 4B. The purified preparation hydrolysed both benzoylcholine and tributyrin. p-Trimethylammoniumanilinium dichloride inhibited non-competitively the hydrolysis of tributyrin and inhibited competitively the splitting of benzoylcholine. The Km value was 0.62 . 10(-3) M for tributyrin and 0.4 . 10(-3) M for benzoylcholine. Antiserum to this purified esterase was prepared in rabbit and it was found that the antiserum did not inhibit esterase activities of human liver, muscle and adipose tissue, although it could inhibit completely the esterase activities of human serum.
D001588:Benzoylcholine / Q000494:pharmacology; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors / Q000097:blood* / Q000302:isolation & purification; D002846:Chromatography, Affinity; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D011487:Protein Conformation; D014280:Triglycerides / Q000494:pharmacology
D014280:Triglycerides; D001588:Benzoylcholine; D002265:Carboxylic Ester Hydrolases; C005830:tributyrin