Somma C, Arnaud J, Boyer J
Acta Haematol. 1983;70(5):337-40. doi: 10.1159/000206770.
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.
人类红细胞（RBC）中存在二酯脂肪酶活性。二酯脂肪酶活性作为一种膜结合酶，以完整的红细胞作为酶源进行测定。二 - [³H] - 油酰甘油（0.6 mM）乳液用作底物。该反应的最适pH在37℃时为7.8。经过两步纯化程序后，通过定量孵育20分钟期间释放的[³H] - 油酸量来监测脂解速率。[³H] - 油酸首先通过液 - 液分配系统从孵育混合物中提取，然后通过薄层色谱进一步分离。从36名健康成年受试者获得的纯化红细胞悬液的二酯脂肪酶活性为196±（标准差）45 mU / 10¹²个红细胞，男性和女性之间无差异。
