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P i ∠ATP exchange in the absence of proton gradient by the H + ‐ATPase from yeast plasma membranes
Author(s) -
de Meis Leopoldo,
Blanpain Jean-Philippe,
Goffeau André
Publication year - 1987
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(87)81369-8
Subject(s) - yeast , membrane , atpase , chemistry , proton , plasma , f atpase , saccharomyces cerevisiae , proton pump , biochemistry , biophysics , enzyme , physics , biology , nuclear physics , thylakoid , chloroplast , gene
Purified soluble H + ‐ATPase from Schizosaccharomyces pombe catalyzes a P i ∠ATP exchange in the absence of a H + gradient. When the pH of the assay medium is raised from 5.5 to 8.0 there is a decrease of the ATPase activity and an increase of the rate of P i ∠ATP exchange. At pH 7.0 the addition of the organic solvent dimethyl sulfoxide (20%,) promotes a decrease of ATPase activity and an increase of the P i ∠ATP exchange reaction. The effect of the organic solvent on the P i ∠ATP exchange is related to a decrease of the apparent K m for P i .

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