Article
The glucose transport activity of GLUT1 is markedly decreased by substitution of a single amino acid with a different charge at residue 415.
Biochemical and biophysical research communications - 30 Apr 1991
Ishihara H, Asano T, Katagiri H, Lin J L, Tsukuda K, Shibasaki Y, Yazaki Y, Oka Y
Abstract excerpt
GLUT1 glucose transporter cDNA was modified to introduce a single amino acid substitution of aspartic acid for asparagine 415, which is conserved among all facilitative glucose transporter isoforms. Although a significant amount of the mutated transporter was expressed into plasma membranes of Ch...
Topics
- Animals
- Asparagine
- Aspartic Acid
- Binding Sites
- Cell Membrane
- Cells, Cultured
- Cricetinae
- Cricetulus
- Cytochalasin B
- DNA
- Deoxyglucose
- Glucose
- Kinetics
- Monosaccharide Transport Proteins
- Mutation