The Journal of biological chemistry, 267(25), 17502-17507 (1992-09-05)
The structure-function relationship of the HepG2/erythrocyte-type glucose transporter (GLUT1) has been studied by in vitro site-directed mutagenesis. Chinese hamster ovary clones in which glucose transporters were transfected were shown by Western blotting with a GLUT1 anti-COOH-terminal peptide antibody to have
The Journal of membrane biology, 123(3), 191-207 (1991-09-01)
We have previously shown that the human red cell glucose transport protein and the anion exchange protein, band 3, are in close enough contact that information can be transmitted from the glucose transport protein to band 3. The present experiments
Two triple cysteine mutants containing Cys-less N- or C-terminal halves and the Cys-less GLUT1 were generated by site-directed mutagenesis. Following expression in Xenopus oocytes, the intrinsic transport activities of the multiple cysteine mutants were slightly decreased when either the cysteine
Journal of developmental physiology, 11(3), 159-169 (1989-03-01)
The effects of insulin, prostaglandin E1 (PGE1) and uptake inhibitors on unidirectional D-glucose influx at brush border (maternal) and basal (fetal) sides of the guinea-pig syncytotrophoblast were investigated in the intact, perfused guinea-pig placenta by rapid, paired-tracer dilution. Experiments were
The Journal of biological chemistry, 260(8), 4575-4578 (1985-04-25)
The stopped flow method combined with fluorescence detection has been employed to study the rapid kinetics of the glucose transporter from human erythrocytes. Upon mixing the purified transporter reconstituted into unsealed membranes of erythrocyte lipids with 4,6-ethylidene D-glucose, a derivative
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