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
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
The effect of ligands on the tryptophan fluorescence of the purified monosaccharide transporter from human erythrocytes has been investigated. Cytochalasin B, D-glucose, and ethylideneglucose quench the fluorescence of the protein at longer wavelengths by 17%, 13%, and 8%, respectively. Propyl
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
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