Purification, properties, and substrate specificity of a carboxylesterase in pancreatic juice.
An esterase activity was purified from rat pancreatic juice by DEAE cellulose chromatography, hydroxylapatite chromatography, and filtration through Sephadex G-100. After this procedure the enzyme was purified 200 times with a yield of 12%. The enzyme had a molecular weight of around 70,000 and an isoelectric point of 5.0. It had a wide substrate specificity and hydrolysed water-soluble esters as well as water-insoluble esters when dispersed with bile salt. Bile salt strongly stimulated the esterase activity, caused aggregation of the enzyme monomer into a polymer form, and protected the activity against proteolytic inactivation. On the basis of the low substrate specificity, the enzyme should be classified as a carboxylic esterase. It most probably is identical with sterolester hydrolase.
D000818:Animals; D001647:Bile Acids and Salts / Q000494:pharmacology; D002264:Carboxylic Acids; D004950:Esterases / Q000302:isolation & purification* / Q000378:metabolism; D006868:Hydrolysis; D008970:Molecular Weight; D010189:Pancreatic Juice / Q000201:enzymology*; D051381:Rats; D013268:Stimulation, Chemical
D001647:Bile Acids and Salts; D002264:Carboxylic Acids; D004950:Esterases