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H + /ion antiport as the principal mechanism of transport systems in the vacuolar membrane of the yeast Saccharomyces carlsbergensis
Author(s) -
Okorokov L.A.,
Kulakovskaya T.V.,
Lichko L.P.,
Polorotova E.V.
Publication year - 1985
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(85)80130-7
Subject(s) - antiporter , antiporters , yeast , vacuole , chemistry , ion transporter , membrane , electrochemical gradient , membrane transport , atpase , saccharomyces cerevisiae , biophysics , biochemistry , enzyme , biology , cytoplasm
The secondary transport systems of the yeast vacuolar membrane have been investigated by (i) the method of radioactive isotopes ([ 14 C]arginine); (ii) activation of H + ‐ATPase by cations (Cat + ), when the enzyme is under H + control and (iii) measurement of changes in the proton gradient (Δ pH) and membrane potential ( E m ) due to the supposed substrates of the transporters. The main mechanism of cation transport across the yeast tonoplast is probably H + /Cat + antiport. The apparent K m of antiporters for Ca 2+ , Mg 2+ Mn 2+ , Zn 2+ and P i are 0.06, 0.3, 0.8, 0.055‐0.17 and 1.5mM, respectively.