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Articles

Purification, Properties, and Substrate Specificity of a Carboxylesterase in Pancreatic Juice

Pages 401-408 | Received 27 Nov 1974, Accepted 14 Feb 1975, Published online: 16 Oct 2020
 

Abstract

Erlanson, C. Purification, properties, and substrate specificity of a carboxylesterase in rat pancreatic juice. Scand. J. Gastroent. 1975, 10, 401-408.

An esterase activity was purified from rat pancreatic juice by DEAE celulose 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.

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