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PMID: 1699808 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

A mitochondrial protein fraction catalyzing transport of the K+ analog T1+.

FEBS letters ·Vol. 273 ·No. 1-2 ·1990-10-29 ·Pages 215-8

Diwan JJ, Paliwal R, Kaftan E, Bawa R

Abstract

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.

MeSH Terms
Aldehyde Dehydrogenase/chemistry,metabolism Animals Biological Transport, Active Epitopes/analysis Fluorescent Dyes Kinetics Membrane Proteins/genetics,metabolism Mitochondria, Liver/metabolism Molecular Weight Potassium/metabolism Rats Submitochondrial Particles/metabolism Thallium/metabolism Valinomycin/pharmacology
Chemicals
Epitopes Fluorescent Dyes Membrane Proteins Valinomycin Thallium Aldehyde Dehydrogenase Potassium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Diwan J J
Biology Department, Rensselaer Polytechnic Institute, Troy, NY 12180-3590.
Paliwal R
Kaftan E
Bawa R
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1990-10-29
Pages
215-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NIGMS NIH HHS · GM-20726 · United States
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