与人类多形核白细胞膜相关的磷脂酶A活性。
Phospholipase A activity associated with membranes of human polymorphonuclear leucocytes.
作者信息
Franson R, Weiss J, Martin L, Spitznagel J K, Elsbach P
出版信息
Biochem J. 1977 Dec 1;167(3):839-41. doi: 10.1042/bj1670839.
Abstract
Homogenates of human polymorphonuclear leucocytes (granulocytes) contain a Ca2+-dependent phospholipase A with optimal activity pH7.0. This enzyme is membrane-bound and is enriched in crude cytoplasmic-granule fraction. Ratezonal centrifugation of the cytoplasmic-granule fraction demonstrates that the phospholipase A is associated not only with specific- and azurophilic-granule populations but also with an 'empty' vesicular fraction containing 85% of the total alkaline phosphatase activity of whole homogenate. Thus this phospholipase is associated with granule as well as with other cellular membranes of human granulocytes.
摘要
人多形核白细胞（粒细胞）匀浆含有一种Ca2+依赖性磷脂酶A，其最适活性pH为7.0。这种酶与膜结合，在粗制细胞质颗粒组分中含量丰富。细胞质颗粒组分的速率区带离心表明，磷脂酶A不仅与特异性颗粒和嗜天青颗粒群体相关，还与一个“空”泡状组分相关，该组分含有全匀浆总碱性磷酸酶活性的85%。因此，这种磷脂酶与人类粒细胞的颗粒以及其他细胞膜相关。
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