IDENTIFICATION OF ANTIGEN 19/27 AS DIHYDROLIPOYL DEHYDROGENASE AND ITS PROBABLE INVOLVEMENT IN UBIQUINONE‐MEDIATED NADH‐DEPENDENT TRANSPORT PHENOMENA IN MEMBRANE VESICLES OF ESCHERICHIA COLI
IDENTIFICATION OF ANTIGEN 19/27 AS DIHYDROLIPOYL DEHYDROGENASE AND ITS PROBABLE INVOLVEMENT IN UBIQUINONE‐MEDIATED NADH‐DEPENDENT TRANSPORT PHENOMENA IN MEMBRANE VESICLES OF ESCHERICHIA COLI
复制标题
抗原 19/27 作为二氢丙酰脱氢酶的鉴定及其可能参与大肠杆菌膜囊泡中泛醌介导的 NADH 依赖性转运现象
DOI：
10.1111/j.1574-6941.1980.tb01619.x
复制
发表时间：
1980
影响因子：
2.1
通讯作者：
K. Graeme
中科院分区：
文献类型：
--
作者：
P. Owen;H. Kaback;K. Graeme
虽然NADH脱氢酶（EC 1.6. 99.3）的研究（综述见[1]），但很少能实现催化物质的明确分离。关于酶是否是质子移位的证据也存在矛盾[2-41]。近年来，我们应用交叉免疫电泳（CIE）技术对大肠杆菌转运膜囊泡中的抗原进行了分析。coliML 308 -225，并且能够清楚地分辨具有NADH-四唑还原酶活性的两种酶（5;参见图1Az）。一种抗原（称为15号）几乎仅在细胞的膜部分中分配[6]，并且能够氧化NADH和NADPH [11]。抗原15也似乎是主要的含铁膜免疫原，如从用源自在1Fe [1]存在下生长的细胞的囊泡进行的CIE实验所判断的。第二种免疫学上不同的酶似乎是抗原复合物的一部分，被称为抗原19/27 [5，6]。它在膜和细胞质之间以相似的程度分级分离[6]，并且可以通过其不能氧化NADPH和不存在结合铁而进一步与抗原15区分[13]。在本通讯中，我们进一步报告了这两种酶的性质及其在NADH依赖性转运现象中的可能作用。
Although the NADH dehydrogenase (EC 1.6. 99.3) from Escherichia coli has been studied by several investigators (reviewed in [l]), clear resolution of the catalytic species has rarely been achieved. There is also conflicting evidence as to whether the enzyme is proton translocating or not [2-41. Recently, we applied the powerful technique of crossed immunoelectrophoresis (CIE) to the analysis of antigens present in transporting membrane vesicles of E. coli ML308-225 and were able to resolve clearly two enzymes possessing NADH-tetrazolium reductase activity (5; see Fig. lAz). One antigen (termed no. 15) partitioned almost exclusively in the membrane fraction of the cell [6] and was capable of oxidizing both NADH and NADPH [1 1. Antigen 15 also appeared to be the major iron-containing membrane immunogen as judged from CIE experiments conducted with vesicles derived from cells grown in the presence of" Fe [l]. A second immunologically distinct enzyme appeared to be part of an antigen complex and was termed antigen 19/27 [5, 6]. It fractionated to similar extents between the membrane and cytoplasm [6] and could be further differentiated from antigen 15 by its inability to oxidise NADPH and by the absence of bound iron [13. In the present communication we report further on the properties of these two enzymes and on their probable roles in NADH-dependent transport phenomena in