Diwan J J, Paliwal R, Kaftan E, Bawa R
Biology Department, Rensselaer Polytechnic Institute, Troy, NY 12180-3590.
FEBS Lett. 1990 Oct 29;273(1-2):215-8. doi: 10.1016/0014-5793(90)81088-6.
A protein fraction has been obtained from detergent-solubilized mitochondrial membranes by its affinity for quinine, an inhibitor of K+ transport. A peptide derived from the predominant 53 kDa protein in this fraction is found to be identical in sequence to a portion of aldehyde dehydrogenase. Antigenically unrelated bands at 97, 77, 57, and 31 kDa are also seen on polyacrylamide gels. Observations utilizing a fluorescent probe entrapped in the lumen of membrane vesicles indicate that the reconstituted protein fraction imparts permeability to the K+ analog Tl+. These and other findings suggest that the affinity purified fraction includes a cation transport catalyst.
通过对钾离子转运抑制剂奎宁的亲和力，从经去污剂溶解的线粒体膜中获得了一种蛋白质组分。发现该组分中主要的53 kDa蛋白质衍生的肽段在序列上与醛脱氢酶的一部分相同。在聚丙烯酰胺凝胶上还可见到97 kDa、77 kDa、57 kDa和31 kDa的抗原无关条带。利用包埋在膜泡腔中的荧光探针进行的观察表明，重组后的蛋白质组分赋予钾离子类似物铊离子通透性。这些以及其他发现表明，亲和纯化的组分包含一种阳离子转运催化剂。
