Purification of an enzyme with lysophospholipase activity from rat intestinal mucosa by hydrophobic chromatography

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 subsodium dodecyl sulphate gel electrophoresis; its isoelectric point is 5.6.