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A mitochondrial protein fraction catalyzing transport of the K + analog Tl +
Author(s) -
Diwan Joyce Johnson,
Paliwal Ranjana,
Kaftan Edward,
Bawa Raj
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81088-6
Subject(s) - chemistry , fraction (chemistry) , radiochemistry , chromatography
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.