rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1991-8-15
|
pubmed:abstractText |
The existence of an endogenous Na(+)-glutamate cotransporter in the oocytes of Xenopus laevis is demonstrated. The transporter does not accept D-glutamate as substrate. The dependence on substrate displays two saturating components with low (K1/2 = 9 mM) and high (K1/2 = 0.35 microM) affinities for L-glutamate. The dependence on external Na+ exhibits a saturating component with a K1/2 value of about 5 mM and a component that has not saturated up to 110 mM Na+. In voltage-clamped oocytes, it is possible to demonstrate that Na(+)-dependent L-glutamate transport is directly coupled to countertransport of Rb+. The analysis of the voltage dependence of the Na+,K(+)-dependent L-glutamate uptake suggests that positive charges are moved inwardly during the transport cycle.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0006-3002
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
1066
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
14-20
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1676599-Amino Acid Transport System X-AG,
pubmed-meshheading:1676599-Animals,
pubmed-meshheading:1676599-Biological Transport, Active,
pubmed-meshheading:1676599-Carrier Proteins,
pubmed-meshheading:1676599-Electrochemistry,
pubmed-meshheading:1676599-Female,
pubmed-meshheading:1676599-Glutamate Plasma Membrane Transport Proteins,
pubmed-meshheading:1676599-Glutamates,
pubmed-meshheading:1676599-Glutamic Acid,
pubmed-meshheading:1676599-Kinetics,
pubmed-meshheading:1676599-Oocytes,
pubmed-meshheading:1676599-Rubidium,
pubmed-meshheading:1676599-Sodium,
pubmed-meshheading:1676599-Substrate Specificity,
pubmed-meshheading:1676599-Symporters,
pubmed-meshheading:1676599-Xenopus laevis
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pubmed:year |
1991
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pubmed:articleTitle |
Endogenous L-glutamate transport in oocytes of Xenopus laevis.
|
pubmed:affiliation |
Max-Planck-Institut für Biophysik, Frankfurt/Main, F.R.G.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|