A MITOCHONDRIAL PROTEIN-FRACTION CATALYZING TRANSPORT OF THE K+ ANALOG TL+

被引：17

作者：

DIWAN, JJ ^{[1
]}

PALIWAL, R ^{[1
]}

KAFTAN, E ^{[1
]}

BAWA, R ^{[1
]}

机构：

[1] RENSSELAER POLYTECH INST,CTR BIOPHYS,TROY,NY 12180

来源：

FEBS LETTERS | 1990年 / 273卷 / 1-2期

关键词：

Fluorescence quenching; K[!sup]+[!/sup] transport; Mitochondrial membrane; Quinine; Tl[!sup]+[!/sup;

D O I：

10.1016/0014-5793(90)81088-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. © 1990.

引用

页码：215 / 218

页数：4

共 42 条

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[2]

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