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Journal of Lipid Research, Vol. 9, 794-798, November 1968
Copyright © 1968 by Lipid Research, Inc.

Purification of rat pancreatic lipase

Lewis I. Gidez

Institut de Chimie Biologique, Faculté des Sciences, Marseille, France, and Departments of Biochemistry and Medicine, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York 10461

A procedure for the isolation of lipase (glycerolester hydrolase, EC 3.1.1.3) from rat pancreas is described. The purification scheme includes homogenization of the pancreas, centrifugation at 3,000 rpm, centrifugation at 40,000 rpm, DEAE-cellulose chromatography, precipitation of amylase as the amylase-glycogen complex, gel filtration of the amylase-free proteins on Sephadex G-100, and chromatography on carboxymethyl-Sephadex C-50. The enzyme showed only one band on polyacrylamide gel electrophoresis and had a specific activity of 5330 ± 80 units/mg of protein.

Supplementary key words amylase • DEAE-cellulose • Sephadex G-100 • CM-Sephadex C-50

Submitted on May 28, 1968
Accepted on August 13, 1968


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