兔红细胞中与膜相关的NAD⁺糖水解酶可被磷脂酰肌醇特异性磷脂酶C溶解。

Membrane-associated NAD+ glycohydrolase from rabbit erythrocytes is solubilized by phosphatidylinositol-specific phospholipase C.

作者信息

Kim U H, Rockwood S F, Kim H R, Daynes R A

机构信息

Department of Biochemistry, Chonbuk National University Medical School, Chonju, Republic of Korea.

出版信息

Biochim Biophys Acta. 1988 Apr 14;965(1):76-81. doi: 10.1016/0304-4165(88)90153-5.

DOI:10.1016/0304-4165(88)90153-5

PMID:2831996

Abstract

NAD+ glycohydrolase (NADase) present on the surface of rabbit erythrocytes is a membrane-bound ectoenzyme that can be solubilized by phosphatidylinositol-specific phospholipase C (PIPLC). As much as 70% of the cell-associated NADase was made soluble by treatment with PIPLC. The portion of NADase that remained cell-associated after an initial PIPLC treatment proved to be resistant to subsequent solubilization attempts. Further analysis showed that release of NADase from erythrocytes could not be attributed to the action of proteinases or phospholipase C. Erythrocytes obtained from other mammals were analyzed and found to have variable amounts of PIPLC-susceptible NADase. Practically, this finding can be used to easily solubilize membrane-bound NADase as a first step in its purification.

摘要

存在于兔红细胞表面的NAD⁺糖水解酶（NADase）是一种膜结合外切酶，可被磷脂酰肌醇特异性磷脂酶C（PIPLC）溶解。用PIPLC处理后，多达70%与细胞相关的NADase可被溶解。在最初的PIPLC处理后仍与细胞相关的那部分NADase被证明对随后的溶解尝试具有抗性。进一步分析表明，NADase从红细胞中的释放不能归因于蛋白酶或磷脂酶C的作用。对从其他哺乳动物获得的红细胞进行分析，发现其具有不同量的对PIPLC敏感的NADase。实际上，这一发现可用于轻松溶解膜结合的NADase，作为其纯化的第一步。