E32754
4,6-O-Ethyliden-α-D-Glukose
Synonym(e):
4,6-O-Ethyliden-α-D-glucopyranose, Ethylidenglucose, NSC 89726
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Über diesen Artikel
Empirische Formel (Hill-System):
C8H14O6
CAS-Nummer:
Molekulargewicht:
206.19
NACRES:
NA.22
PubChem Substance ID:
UNSPSC Code:
12352200
EC Number:
236-198-2
MDL number:
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Unterstützung erhaltenInChI key
VZPBLPQAMPVTFO-NKWOADHPSA-N
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
SMILES string
CC1OC[C@H]2O[C@H](O)[C@H](O)[C@@H](O)[C@@H]2O1
mp
168-170 °C (lit.)
1 of 4
Dieser Artikel | 05389 | 08602 | 292842 |
|---|---|---|---|
| mp 168-170 °C (lit.) | mp - | mp - | mp 164-165 °C (lit.) |
Lagerklasse
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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F R Gorga et al.
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
A Janoshazi et al.
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
G F Baker et al.
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
J R Appleman et al.
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
H Ishihara et al.
Biochemical and biophysical research communications, 176(2), 922-930 (1991-04-30)
GLUT1 glucose transporter cDNA was modified to introduce a single amino acid substitution of aspartic acid for asparagine 415, which is conserved among all facilitative glucose transporter isoforms. Although a significant amount of the mutated transporter was expressed into plasma
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