| Literature DB >> 1699808 |
J J Diwan1, R Paliwal, E Kaftan, R Bawa.
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.Entities:
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Year: 1990 PMID: 1699808 DOI: 10.1016/0014-5793(90)81088-6
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124