Characterization of a diester lipase activity in human erythrocytes

Acta Haematologica
C SommaJ Boyer

Abstract

A diester lipase activity is described in human red blood cells (RBC). Diester lipase activity acts as a membrane-bound enzyme and is assayed using intact RBC as the enzyme source. An emulsion of di-[3H]-oleoylglycerol (0.6 mM) serves as the substrate. The optimum pH for the reaction is 7.8 at 37 degrees C. Lipolytic rates are monitored by quantitation of the amount of [3H]-oleic acid released during 20 min of incubation after a two-step purification procedure. [3H]-oleic acid is first extracted from the incubation mixture by means of a liquid-liquid partition system and further isolated by thin-layer chromatography. Suspensions of purified RBC obtained from 36 healthy adult subjects had a diester lipase activity of 196 +/- (SD) 45 mU/10(12) RBC, with no difference between men and women.

Citations

Jan 1, 1985·The International Journal of Biochemistry·M FujiiK Koga
Jan 1, 1986·The International Journal of Biochemistry·M FujiiK Koga
Dec 1, 1986·Alcoholism, Clinical and Experimental Research·C DelpéroJ Boyer

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