人类红细胞中的α-甘露糖苷酶

Alpha-mannosidase in human red cells.

Poenaru L, Dreyfus J C

Biochim Biophys Acta. 1979 Jan 12;566(1):67-71. doi: 10.1016/0005-2744(79)90249-3.

Abstract

A search for lysosomal hydrolases and related enzymes has been made in hemolysates from human and rabbit red cells. Apart from acid phosphatases, significant activities were found only for alpha-mannosidase, neutral alpha-glucosidase and beta-hexosaminidase. 2. alpha-Mannosidase (alpha-D-mannoside mannohydrolase, EC 3.2.1.24) activity per cell in human red blood cells was 200-times lower than in white cells. The optimal pH was 5.5--6.0. Electrophoresis on cellulose acetate showed three bands. Hemolysates from four patients with mannosidosis were not deficient in alpha-mannosidase. pH activity curves and elctrophoretic pattern were similar to those of controls. From its biochemical and genetic properties, it is concluded that red cell mannosidase differs from the lysosomal acid mannosidase.

摘要

已对人及兔红细胞溶血产物中的溶酶体水解酶及相关酶进行了搜寻。除酸性磷酸酶外，仅发现α-甘露糖苷酶、中性α-葡糖苷酶和β-己糖胺酶有显著活性。2. 人红细胞中每个细胞的α-甘露糖苷酶（α-D-甘露糖苷甘露水解酶，EC 3.2.1.24）活性比白细胞低200倍。最适pH为5.5 - 6.0。在醋酸纤维素上电泳显示出三条带。四名甘露糖苷贮积症患者的溶血产物中α-甘露糖苷酶并不缺乏。pH活性曲线和电泳图谱与对照组相似。从其生化和遗传特性得出结论，红细胞甘露糖苷酶与溶酶体酸性甘露糖苷酶不同。