Grebing C, Crane F L, Löw H, Hall K
J Bioenerg Biomembr. 1984 Dec;16(5-6):517-33. doi: 10.1007/BF00743243.
Evidence is presented for a transmembranous NADH-dehydrogenase in human erythrocyte plasma membrane. We suggest that this enzyme is responsible for the ferricyanide reduction by intact cells. This NADH-dehydrogenase is distinctly 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 microM for NADH and 125 microM for ferricyanide. It is inhibited by p-chloromercuribenzoate, bathophenanthroline sulfonate, and chlorpromazine.
有证据表明人红细胞质膜中存在一种跨膜NADH脱氢酶。我们认为这种酶负责完整细胞对铁氰化物的还原作用。这种NADH脱氢酶与膜细胞质侧的NADH - 细胞色素b5还原酶明显不同。用非渗透性抑制剂重氮苯磺酸盐（DABS）预处理红细胞会导致分离的质膜中NADH - 铁氰化物还原酶活性丧失35%。由于NADH和铁氰化物都不能透过细胞膜，跨膜酶只能在两个表面都暴露的开放膜片中进行测定，而不能在封闭的囊泡中测定。跨膜脱氢酶对NADH的亲和常数为90微摩尔，对铁氰化物的亲和常数为125微摩尔。它受到对氯汞苯甲酸、磺酸浴菲罗啉和氯丙嗪的抑制。
