Characterization of functional human erythrocyte-type glucose transporter (GLUT1) expressed in insect cells using a recombinant baculovirus.
The human erythrocyte-type glucose transporter (GLUT1) has been abundantly expressed in insect cells by using a recombinant baculovirus. At 4 days after infection with the virus, the insect cell-surface and intracellular membranes were found to contain greater than 200 pmol of D-glucose-sensitive binding sites for the transport inhibitor cytochalasin B per mg of protein. The characteristics of binding were identical with those of the erythrocyte transporter, although the two proteins differed substantially in apparent Mr, probably as a result of glycosylation differences.
Yi
C K
CK
Department of Biochemistry, Royal Free Hospital School of Medicine, University of London, U.K.
Charalambous
B M
BM
Emery
V C
VC
Baldwin
S A
SA
D000818:Animals; D016367:Baculoviridae / Q000235:genetics*; D015153:Blotting, Western; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D003571:Cytochalasin B / Q000378:metabolism; D004274:DNA, Recombinant; D004912:Erythrocytes / Q000737:chemistry*; D005455:Fluorescent Antibody Technique; D015870:Gene Expression; D005822:Genetic Vectors; D006031:Glycosylation; D006801:Humans; D008970:Molecular Weight; D009004:Monosaccharide Transport Proteins / Q000235:genetics* / Q000378:metabolism; D009036:Moths / Q000378:metabolism*; D014162:Transfection
D004274:DNA, Recombinant; D009004:Monosaccharide Transport Proteins; D003571:Cytochalasin B