1887

Abstract

To identify the putative lactate transporter protein of , plasma membranes from cells grown either on lactic acid (presence of lactate proton symport) or glucose (absence of lactate proton symport) were incubated with –[U–C]lactic acid and the membrane proteins were then separated by SDS-PAGE. A well-defined peak of radioactivity occurred in the lane of the gel containing plasma membrane proteins from lactic-acid-grown cells but not from glucose-grown cells. Binding was inhibited by unlabelled pyruvate and lactate, whereas succinate and citrate were not inhibitory. The monocarboxylate transporter inhibitor of animal cells, 4,4′-diisothiocyanato-stilbene-2,2′-disulfonate, competitively inhibited the lactate proton symport in the whole yeast and also inhibited lactate binding to proteins of isolated plasma membranes. The polypeptide pattern of plasma membranes from lactic-acid-grown cells revealed a 43 kDa polypeptide associated with the peak of labelled lactate. Altogether the results suggest that this polypeptide is either the lactate transporter or a component of it.

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2000-03-01
2024-04-19
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