Purification of an Enzyme with Lysophospholipase Activity from Rat Intestinal Mucosa by Hydrophobic Chromatography

Stig Allenmark Clinical Research Centre, University of Linköping, S-581 85, Linköping

Eva Sjödahl Department of Surgery, University of Linköping, S-581 85, Linköping

Rune Sjödahl Department of Surgery, University of Linköping, S-581 85, Linköping

Christer Tagesson Department of Clinical Chemistry, University of Linköping, S-581 85, Linköping

Abstract

A method based on hydrophobic chromatography is described for the purification of a lysophospholipase from the mucosa of rat small intestine. Under the conditions used, one single chromatographic run on phenyl-Sepharose CL-4B yielded a 582-fold purification with a 79% overall recovery of enzyme activity. A sub-unit molecular weight of 56,000 was deduced from sodium dodecyl sulphate gel electrophoresis; its isoelectric point is 5.6.

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Purification of an Enzyme with Lysophospholipase Activity from Rat Intestinal Mucosa by Hydrophobic Chromatography

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Purification of an Enzyme with Lysophospholipase Activity from Rat Intestinal Mucosa by Hydrophobic Chromatography

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