Sterol ester hydrolytic activity of lipoprotein lipase from Pseudomonas fluorescence.

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Abstract
Sterol ester hydrolase activity was found in the crude enzyme preparation of lipoprotein lipase from P. fluorescens. The enzyme was purified by (NH4)2SO4 fractionation and chromatography on DEAE-cellulose, Sephadex G-75 and CM-cellulose. The lipolytic activity and sterol ester hydrolytic activity at various stages in the purification were found in the same fraction, and the ratio of both activities was constant. The purified enzyme was homogeneous by disc electrophoresis and SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis. One single protein peak which contained lipolytic and sterol ester hydrolytic activities was observed by isoelectric focusing. The actions of lipoprotein lipase and sterol ester hydrolase apparently belong to a same enzyme protein. The action of the purified enzyme for the cholesterol esters in human plasma was investigated. Cholesterol ester was hydrolyzed completely, and the rate of hydrolysis of esters of long chain fatty acids was more rapid than that of short.

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