Article
Substitution of leucine for tryptophan 412 does not abolish cytochalasin B labeling but markedly decreases the intrinsic activity of GLUT1 glucose transporter.
The Journal of biological chemistry - 25 Apr 1991
Katagiri H, Asano T, Shibasaki Y, Lin J L, Tsukuda K, Ishihara H, Akanuma Y, Takaku F, Oka Y
Abstract excerpt
GLUT1 glucose transporter cDNA was modified to introduce a single amino acid substitution of leucine for tryptophan 412, a putative cytochalasin B photo-affinity labeling site. Although the mutated transporter was expressed into plasma membranes of Chinese hamster ovary cells, glucose transport activity of the mutated transporter was observed to be only 15-30% of that of the wild-type GLUT1 when glucose transport...
Topics
- Affinity Labels
- Animals
- Blotting, Western
- Cricetinae
- Cricetulus
- Cytochalasin B
- Deoxyglucose
- Electrophoresis, Polyacrylamide Gel
- Gene Expression Regulation
- Leucine