A TRANSMEMBRANOUS NADH-DEHYDROGENASE IN HUMAN-ERYTHROCYTE MEMBRANES
A TRANSMEMBRANOUS NADH-DEHYDROGENASE IN HUMAN-ERYTHROCYTE MEMBRANES
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DOI：
10.1007/bf00743243
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发表时间：
1984-01-01
影响因子：
3
通讯作者：
HALL, K
中科院分区：
文献类型：
--
作者：
GREBING, C;CRANE, FL;HALL, K
证据提出了跨膜nadh脱氢酶在人红细胞膜。显然，这种酶负责完整细胞的铁氨酸还原。这种nadh脱氢酶与细胞膜细胞质侧的nadh细胞色素b5还原酶明显不同。用非穿透性抑制剂重氮苯磺酸盐（DABS）预处理红细胞导致分离的质膜中nadh -铁氰化物还原酶活性降低35%。由于NADH和铁氰化物都是不可渗透的，跨膜酶只能在开放的膜片中检测，表面都暴露在外，而不能在封闭的囊泡中检测。跨膜脱氢酶的亲和常数为90 .mu。NADH为M， 125 .mu。M代表氰化铁。对氯苯甲酯、邻苯二甲酸乙酯和氯丙嗪对其有抑制作用。
Evidence is presented for a transmembranous NADH-dehydrogenase in human erythrocyte plasma membrane. Apparently, this enzyme is responsible for the ferricyaninde reduction by intact cells. This NADH-dehydrogenase is distinct different from the NADH-cytochrome b5 reductase on the cytoplasmic side of the membrane. Pretreatment of erythrocytes with the nonpenetrating inhibitor diazobenzene sulfonate (DABS) results in a 35% loss of NADH-ferricyanide reductase activity in the isolated plasma membrane. Since NADH and ferricyanide are both impermeable, the transmembrane enzyme can only be assayed in open membrane sheets with both surfaces exposed, and not in closed vesicles. The transmembrane dehydrogenase has affinity constants of 90 .mu.M for NADH and 125 .mu.M for ferericyanide. It is inhibited by p-chloromercuribenzoate, bathophenanthroline sulfonate, and chlorpromazine.