Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 146 (2000), 695-699
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gerós, H.
Right arrow Articles by Leão, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gerós, H.
Right arrow Articles by Leão, C.
Agricola
Right arrow Articles by Gerós, H.
Right arrow Articles by Leão, C.
Microbiology (2000), 146, 695-699.
© 2000 Society for General Microbiology

Bioenergetics and Transport

L–[U–14C]Lactate binding to a 43 kDa protein in plasma membranes of Candida utilis

Hernâni Gerós1, Fátima Baltazar1, Fernanda Cássio1 and Cecília Leão1

Centro de Ciências do Ambiente, Departamento de Biologia, Universidade do Minho, 4710-057 Braga, Portugal1

Author for correspondence: Fernanda Cássio. Tel: +351 253604310. Fax: +351 253678980. e-mail: fcassio{at}bio.uminho.pt

To identify the putative lactate transporter protein of Candida utilis, plasma membranes from cells grown either on lactic acid (presence of lactate proton symport) or glucose (absence of lactate proton symport) were incubated with L–[U–14C]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.

Keywords: affinity labelling, lactate transporter, Candida utilis

Abbreviations: DIDS, 4,4'-diisothiocyanatostilbene-2,2'-disulfonate; MCT, monocarboxylate transporter






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2000 Society for General Microbiology.