The competitive inhibition of glucose transport in human erythrocytes by compounds of different structures.
By kinetic analysis we found that the transport protein for glucose in human erythrocyte membranes has different binding sites for competitive inhibitors. They all change the transport protein with the effect that it loses its affinity to glucose. Some of the competitive inhibitors alter the conformation of the transport protein, so that other ones cannot be bound. There are inhibitors, however, which do not affect the affinity of other competitive inhibitors. A schematic model of our assumption about the mechanism of the competitive inhibition of glucose transport is presented.
D001667:Binding, Competitive; D001786:Blood Glucose / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism*; D000431:Ethanol / Q000097:blood; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008320:Maltose / Q000097:blood; D008956:Models, Chemical; D014364:Tryptophan / Q000031:analogs & derivatives / Q000097:blood
D001786:Blood Glucose; D001798:Blood Proteins; D002352:Carrier Proteins; D000431:Ethanol; D008320:Maltose; C028129:tryptophan methyl ester; D014364:Tryptophan