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Dependence of the kinetics of secondary active transports in yeast on H(+)-ATPase acidification

The Journal of Membrane Biology

Feb 1, 1994

A Kotyk

PMID: 8189429

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Abstract

Acidification of the external medium of the yeast Saccharomyces cerevisiae, mainly caused by proton extrusion by plasma membrane H(+)-ATPase, was inhibited to different degrees by D2O, diethylstilbestrol, suloctidil, vanadate, erythrosin B, cupric sulfate and dicyclohexylcarbodiimide. T...read more

Mentioned in this Paper

Suloctidil
Saccharomyces cerevisiae allergenic extract
Adenosine Triphosphatases
Amino Acids, I.V. solution additive
Resting Potentials
Uptake
Phosphate Measurement
Acidification - ActCode
Etiology
Copper Sulfate
Paper Details
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J C García, A Kotyk
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Dependence of the kinetics of secondary active transports in yeast on H(+)-ATPase acidification

The Journal of Membrane Biology

Feb 1, 1994

A Kotyk

PMID: 8189429

DOI:

Abstract

Acidification of the external medium of the yeast Saccharomyces cerevisiae, mainly caused by proton extrusion by plasma membrane H(+)-ATPase, was inhibited to different degrees by D2O, diethylstilbestrol, suloctidil, vanadate, erythrosin B, cupric sulfate and dicyclohexylcarbodiimide. T...read more

Mentioned in this Paper

Suloctidil
Saccharomyces cerevisiae allergenic extract
Adenosine Triphosphatases
Amino Acids, I.V. solution additive
Resting Potentials
Uptake
Phosphate Measurement
Acidification - ActCode
Etiology
Copper Sulfate

Feeds With Similar Papers

ATP Synthases

ATP synthases are enzymes located in the inner mitochondrial membrane that catalyze the synthesis of ATP during cellular respiration. Discover the latest research on ATP synthases here.

Related Papers

Folia Microbiologica

Uptake of L-lysine by a double mutant of Saccharomyces cerevisiae

Folia MicrobiologicaJanuary 1, 1988
J C García, A Kotyk
Paper Details
References
  • References
  • Citations6
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations6
1

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