Bry K, Andersson L C, Kuusi T, Kinnunen P K
Biochim Biophys Acta. 1979 Oct 26;575(1):121-7. doi: 10.1016/0005-2760(79)90137-1.
In the present paper we show for the first time monoacylglycerol hydrolase in human platelets. No monoacylglycerol hydrolase activity could be demonstrated in the other blood cells. The monoacylglycerol hydrolase of platelets could not be released from the cells by heparin, thus the enzyme is distinct from the postheparin plasma lipases. The enzyme could be solubilized by a non-ionic detergent, Triton X-100. The solubilized monoacylglycerol hydrolase from platelets was optimally active at pH between 7 and 8 and at ionic strength corresponding to [NaCl] between 0.1 and 0.3 M. The optimal assay temperature was 37 degrees C. The enzyme activity was sensitive to HgCl2 but not to NaF. Accordingly, it was stabilized by 2-mercaptoethanol.
在本论文中，我们首次在人血小板中发现了单酰甘油水解酶。在其他血细胞中未检测到单酰甘油水解酶活性。血小板中的单酰甘油水解酶不能被肝素从细胞中释放出来，因此该酶与肝素后血浆脂肪酶不同。该酶可用非离子去污剂Triton X - 100溶解。从血小板中溶解的单酰甘油水解酶在pH值7至8之间以及离子强度相当于0.1至0.3M [NaCl]时活性最佳。最佳测定温度为37℃。该酶活性对HgCl2敏感，但对NaF不敏感。因此，它可被2 - 巯基乙醇稳定。
