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
The Biochemical journal, 295 ( Pt 1), 183-188 (1993-10-01)
The transport conformation of the human erythrocyte glucose transporter (GLUT1) modifies rates of proteolytic cleavage of this protein by a variety of enzymes. We investigated the effects of ligand-induced conformational change on the susceptibility to enzymic cleavage of the insulin-sensitive
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
Molecular and cellular endocrinology, 62(2), 153-159 (1989-04-01)
4,6-O-Ethylidene glucose (ethylidene glucose), a specific inhibitor at the outer surface of a glucose transporter in the cell membranes, substituted analogue of streptozotocin was newly synthesized. This compound did not induce diabetes in rats and also did not show cytotoxic
The Journal of endocrinology, 112(3), 375-378 (1987-03-01)
Ethylidene glucose (4,6-O-ethylidene glucose; EG) is known to bind the outer surface of the glucose transporter in the membranes of human erythrocytes and other mammalian cells. If a glucose transport system is present on pancreatic beta cells and recognizes the
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