Functional effects and cross-reactivity of antibody to purified subunit b (uncF protein) of Escherichia coli proton-ATPase.
Functional effects and cross-reactivity of antibody to purified subunit b (uncF protein) of Escherichia coli proton-ATPase.
复制标题
抗体对大肠杆菌质子-ATP 酶纯化亚基 b（uncF 蛋白）的功能影响和交叉反应性。
DOI：
10.1016/0003-9861(85)90664-2
复制
发表时间：
1985
影响因子：
3.9
通讯作者：
Senior,AE
中科院分区：
文献类型：
--
作者：
Perlin,DS;Senior,AE
Subunit b (uncFprotein) of the proton-ATPase (F1F0) ofEscherichia coliwas purified from membranes of strain AN1460 (unc+). Antibody to purified subunit b was raised in rabbits. It reacted with F1-depleted membranes and blocked F1binding. Bound antibody had no effect on proton transport through F0. F1-Depleted membranes competed with purified subunit b for antibody in an enzyme-linked immunosorbent assay. F1-Depleted membranes which had been pretreated with trypsin or preincubated with saturating amounts of soluble F1competed poorly with purified subunit b for antibody. The antibody to subunit b was used to further evaluate the trypsin-cleavage data previously reported [D. S. Perlin, D. N. Cox, and A. E. Senior (1983)J. Biol. Chem.258, 9793–9800]. The results indicated that trypsin proteolysis of F1-depleted membranes resulted in the transient appearance of three fragments of subunit b (Mr= 16,400, 15,700, and 15,500) that remained tightly bound to the membrane. A water-soluble fragment (Mr14,800), previously thought to be derived from subunit b, was not detected by the antibody. The antibody to subunit b did not cross-react with any subunit of mitochondrial, chloroplast, or other bacterial proton-ATPase, or with the proton-ATPase of clathrin-coated vesicles, plant microsomal membranes, orNeurospora crassaplasma membranes.
