37040
D-(+)-Digitoxose
≥99.0% (TLC)
Sinônimo(s):
2,6-Dideoxy-D-ribohexose
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About This Item
Fórmula empírica (Notação de Hill):
C6H12O4
Número CAS:
Peso molecular:
148.16
Beilstein:
1721555
Número MDL:
Ensaio
≥99.0% (TLC)
atividade óptica
[α]20/D +48±2°, c = 1% in H2O
pf
98-100 °C
cadeia de caracteres SMILES
C[C@H]1OC(O)C[C@H](O)[C@@H]1O
InChI
1S/C6H12O4/c1-3-6(9)4(7)2-5(8)10-3/h3-9H,2H2,1H3/t3-,4+,5?,6-/m1/s1
chave InChI
FDWRIIDFYSUTDP-WGDKFINWSA-N
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Ações bioquímicas/fisiológicas
The natural glycoside digitoxin contains a trisaccharide component made up of digitoxose monosaccharides. A modified monosaccharide digitoxin (with a single digitoxose moiety) was found to have greater anti-proliferative effects on various human non-small cell lung cancer cell lines than intact digitoxin.
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Y Fujii et al.
Biological & pharmaceutical bulletin, 17(4), 467-471 (1994-04-01)
In order to obtain specific antisera to digitoxin, four new types of hapten-bovine serum albumin (BSA) conjugates were synthesized from digitoxin. The haptens were linked to the carrier protein through hemisuccinate and hemisuccinylglycine bridges at the C-3' and C-3" positions
M Hussain et al.
Biochemical and biophysical research communications, 129(2), 358-367 (1985-06-14)
Digitoxose specifically and competitively inhibited glucose stimulated insulin release from islets of both lean and obese mice without affecting either the rate of glucose oxidation or the rate of glucose stimulated oxygen consumption. Obese mouse islets were marginally more resistant
Aaroa P Salas et al.
Molecular microbiology, 58(1), 17-27 (2005-09-17)
The indolocarbazole staurosporine is a potent inhibitor of a variety of protein kinases. It contains a sugar moiety attached through C-N linkages to both indole nitrogen atoms of the indolocarbazole core. Staurosporine biosynthesis was reconstituted in vivo in a heterologous
David L Jakeman et al.
Chemical communications (Cambridge, England), (35)(35), 3738-3740 (2006-10-19)
We report the first 2,6-dideoxysugar-O-glycosyltransferase with substrate flexibility at the 2 position, confirm the function of a putative NDP-hexose 2,3-dehydratase in the jadomycin B biosynthetic gene cluster and deduce the substrate flexibility of downstream enzymes in l-digitoxose assembly, enabling reprogramming
M J Wernke et al.
Biochemical pharmacology, 39(4), 655-659 (1990-02-15)
The purpose of this investigation was to define, under controlled in vitro conditions, the processes contributing to the uptake and accumulation of [3H]digoxin by incubated slices of chicken renal cortex. Progressive uptake was evident in time-course experiments with the slice-to-medium
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