E32754
4,6-O-Ethylidene-α-D-glucose
Synonym(s):
4,6-O-Ethylidene α-D-glucopyranose, Ethylidene glucose, NSC 89726
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About This Item
Recommended Products
mp
168-170 °C (lit.)
SMILES string
CC1OC[C@H]2O[C@H](O)[C@H](O)[C@@H](O)[C@@H]2O1
InChI
1S/C8H14O6/c1-3-12-2-4-7(13-3)5(9)6(10)8(11)14-4/h3-11H,2H2,1H3/t3?,4-,5-,6-,7-,8+/m1/s1
InChI key
VZPBLPQAMPVTFO-NKWOADHPSA-N
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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 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
Biochemistry, 21(8), 1905-1908 (1982-04-13)
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
Biochemistry, 28(20), 8221-8227 (1989-10-03)
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
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