The Journal of membrane biology, 132(2), 167-178 (1993-03-01)
The kinetics of the initial phases of D-glucose binding to the glucose transport protein (GLUT1) of the human red cell can be followed by stopped-flow measurements of the time course of tryptophan (trp) fluorescence enhancement. A number of control experiments
There is considerable evidence that the mechanism of glucose transport by the transporter of human erythrocytes is one in which the transporter oscillates between two conformations, To and Ti. Each conformer possesses a single glucose binding site that in vivo
The Journal of physiology, 395, 57-76 (1988-01-01)
1. Equilibrium exchanges in the range of 2-40 mM-3-O-methyl glucose at 16 degrees C suggested that the half-saturation concentration for exchange was 22 mM and that the maximum velocity (Vmax) was ca. 149 mmol l-1 min-1. 2. Initial rates of
The Journal of biological chemistry, 269(32), 20533-20538 (1994-08-12)
The possible role of 5 transmembrane amino acid residues in the function of the Glut1 glucose transporter was investigated by site-directed mutagenesis. The residues were chosen based on their containing hydroxyl or amide side chains capable of hydrogen bonding to
The Journal of biological chemistry, 259(13), 8125-8133 (1984-07-10)
Irradiation of intact rat adipocytes with high intensity ultraviolet light in the presence of 0.5 microM [3H] cytochalasin B results in the labeling of Mr 43,000 and 46,000 proteins that reside in the plasma membrane fraction. In contrast to the
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