有哪些信誉好的足球投注网站an inverse relationship links temperature and substrate apparent affinity in the ion-coupled cotransporters rgat1 and kaat1反比关系链接温度和衬底表面的亲和力ion-coupled转运蛋白rgat1 kaat1.pdfVIP
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an inverse relationship links temperature and substrate apparent affinity in the ion-coupled cotransporters rgat1 and kaat1反比关系链接温度和衬底表面的亲和力ion-coupled转运蛋白rgat1 kaat1
Int. J. Mol. Sci. 2012, 13, 15565-15574; doi:10.3390/ijms131215565
OPEN ACCESS
International Journal of
Molecular Sciences
ISSN 1422-0067
/journal/ijms
Article
An Inverse Relationship Links Temperature and Substrate
Apparent Affinity in the Ion-Coupled Cotransporters rGAT1
and KAAT1
Antonio Peres *, Alessandra Vollero, Eleonora Margheritis, Francesca D’Antoni and
Elena Bossi
Department of Biotechnology and Life Sciences, University of Insubria, Via Dunant, 3, 21100 Varese,
Italy; E-Mails: alessandra.vollero@uninsubria.it (A.V.); eleonora.margheritis@uninsubria.it (E.M.);
francesca.dantoni@uninsubria.it (F.D.); elena.bossi@uninsubria.it (E.B.)
* Author to whom correspondence should be addressed; E-Mail: antonio.peres@uninsubria.it;
Tel.: +39-0332-421320; Fax: +39-0332-421300.
Received: 19 October 2012; in revised form: 14 November 2012 / Accepted: 15 November 2012/
Published: 22 November 2012
Abstract: The effects of temperature on the operation of two ion-coupled cotransporters of
the SLC6A family, namely rat GAT1 (SLC6A1) and KAAT1 (SLC6A19) from
Manduca sexta , have been studied by electrophysiological means in Xenopus laevis
oocytes expressing these proteins. The maximal transport-associated current (Imax) and the
apparent substrate affinity (K05) were measured. In addition to the expected increase in
transport rate (Q10 = 3–6), both transporters showed greater K05 values (i.e.,
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