Wszystkie zdjęcia(1)
Kluczowe dokumenty
C75004
5-Cholesten-3-one
Synonim(y):
3-Keto-5-cholestene
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About This Item
Polecane produkty
Formularz
powder
Poziom jakości
mp
125-127 °C (lit.)
ciąg SMILES
CC(C)CCC[C@@H](C)[C@H]1CC[C@H]2[C@@H]3CC=C4CC(=O)CC[C@]4(C)[C@H]3CC[C@]12C
InChI
1S/C27H44O/c1-18(2)7-6-8-19(3)23-11-12-24-22-10-9-20-17-21(28)13-15-26(20,4)25(22)14-16-27(23,24)5/h9,18-19,22-25H,6-8,10-17H2,1-5H3/t19-,22+,23-,24+,25+,26+,27-/m1/s1
Klucz InChI
GGCLNOIGPMGLDB-GYKMGIIDSA-N
Kod klasy składowania
11 - Combustible Solids
Klasa zagrożenia wodnego (WGK)
WGK 3
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Środki ochrony indywidualnej
Eyeshields, Gloves, type N95 (US)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Biochimica et biophysica acta, 1145(2), 243-249 (1993-02-09)
In this study we have examined the cholesterol oxidase (Streptomyces cinnamomeus) catalyzed conversion of either 5-cholesten-3 beta-ol or 5-cholesten-3-one into 4-cholesten-3-one in pure sterol or mixed phospholipid-containing monolayers at the air/buffer interface. The mean molecular area requirement of 5-cholesten-3-one in
Biochemistry, 37(51), 17990-18000 (1999-01-28)
Cholesterol oxidase catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one via cholest-5-en-3-one. It has been proposed that His447 acts as the general base catalyst for oxidation, and that the resulting imidazolium ion formed acts as an electrophile for isomerization.
Refolding of a novel cholesterol oxidase from Pimelobacter simplex reveals dehydrogenation activity.
Protein expression and purification, 139, 1-7 (2017-07-18)
Cholesterol oxidases, which catalyze the degradation of cholesterol to cholest-4-en-3-one, are widely used in the pharmaceutical and food processing industries. The cholesterol oxidase from Pimelobacter simplex (PsChO3) was transformed into E. coli BL21(DE3), but it was expressed mainly as inclusion bodies
Bioorganic & medicinal chemistry letters, 8(19), 2663-2668 (1999-01-05)
Cholesterol oxidase stereospecifically isomerizes cholest-5-en-3-one to cholest-4-en-3-one. When the base catalyst for isomerization, Glu361, is mutated to Asp, the rate of deprotonation of cholest-5-en-3-one is not affected, but protonation of the dienolic intermediate becomes rate-limiting. This may be a consequence
Biochimica et biophysica acta. General subjects, 1863(8), 1243-1253 (2019-05-11)
Sterols have been reported to modulate conformation and hence the function of several membrane proteins. One such group is the Chloride Intracellular Ion Channel (CLIC) family of proteins. The CLIC protein family consists of six evolutionarily conserved protein members in
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