Treatment of the human erythrocyte glucose-transport protein with N-ethylmaleimide

1985 ◽  
Vol 13 (4) ◽  
pp. 719-720
Author(s):  
D. A. ELLIOT ◽  
S. A. BALDWIN
Keyword(s):  
Glucose Transport ◽  
Human Erythrocyte ◽  
Transport Protein ◽  
Glucose Transport Protein

Properties of the Human Erythrocyte Glucose Transport Protein Are Determined by Cellular Context†

Biochemistry ◽  
2005 ◽  
Vol 44 (15) ◽  
pp. 5606-5616 ◽  
Author(s):  
Kara B. Levine ◽  
Trista K. Robichaud ◽  
Stephanie Hamill ◽  
Lisa A. Sultzman ◽  
Anthony Carruthers
Keyword(s):  
Glucose Transport ◽  
Human Erythrocyte ◽  
Transport Protein ◽  
Cellular Context ◽  
Glucose Transport Protein

scholarly journals Identification and characterization of the glucose-transport protein of the bovine blood/brain barrier

1987 ◽  
Vol 247 (1) ◽  
pp. 101-108 ◽  
Author(s):  
M A Kasanicki ◽  
M T Cairns ◽  
A Davies ◽  
R M Gardiner ◽  
S A Baldwin
Keyword(s):  
Cerebral Cortex ◽  
Glucose Transport ◽  
Human Erythrocyte ◽  
Glucose Transporter ◽  
Cytochalasin B ◽  
Broad Band ◽  
Transport Protein ◽  
Western Blots ◽  
Glucose Transport Protein

The glucose-transport protein from bovine cerebral-cortex microvessels has been identified and characterized by virtue of its ability to bind the ligand [4-3H]cytochalasin B. Microvessel membranes were found to contain a single set of glucose-inhibitable high-affinity cytochalasin B-binding sites [113 +/- 16 (S.E.M.) pmol/mg of membrane protein], with an association constant of 6.8 +/- 1.8 (S.E.M.) micron-1. D-Glucose inhibited the binding to these sites with a Ki of 31 mM. The transport protein was identified by photoaffinity labelling with [4-3H]cytochalasin B and was found to migrate as a broad band of apparent Mr 55,000 on SDS/polyacrylamide gels. Labelling was inhibited by D-glucose, but not by L-glucose. Treatment with endoglycosidase F yielded a sharper band of apparent Mr 46,000, indicating that the transport protein is glycosylated. However, in contrast with the human erythrocyte glucose transporter, digestion with endo-beta-galactosidase had little effect on the electrophoretic mobility of the microvessel protein. Tryptic digestion of the photolabelled protein yielded a radioactive fragment of apparent Mr 18,000, similar to that of the fragment produced by digestion of the labelled human erythrocyte glucose transporter. In addition, a protein of Mr identical with that of the photolabelled transporter was labelled on Western blots of microvessel membranes by antisera raised against the intact erythrocyte transporter and against synthetic peptides corresponding to its N- and C-terminal regions. It is concluded that the glucose-transport protein of bovine cerebral-cortex microvessel endothelial cells shows structural homology with the human erythrocyte glucose transporter.

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