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D-Gulono-1,4-lactone Sale

(Synonyms: D-(-)-古洛糖酸-gamma-内酯) 目录号 : GC41155

A hexanoic acid

D-Gulono-1,4-lactone Chemical Structure

Cas No.:6322-07-2

规格 价格 库存 购买数量
5g
¥496.00
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10g
¥942.00
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25g
¥2,244.00
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50g
¥3,975.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

D-Gulono-1,4-lactone is a hexanoic acid used as a starting material in enantiomerically pure compound syntheses, including carbohydrate syntheses.

Chemical Properties

Cas No. 6322-07-2 SDF
别名 D-(-)-古洛糖酸-gamma-内酯
Canonical SMILES OC[C@@H](O)[C@]1([H])OC([C@H](O)[C@@H]1O)=O
分子式 C6H10O6 分子量 178.1
溶解度 DMF: 3 mg/ml,DMSO: 3 mg/ml,PBS (pH 7.2): 3 mg/ml 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 5.6148 mL 28.0741 mL 56.1482 mL
5 mM 1.123 mL 5.6148 mL 11.2296 mL
10 mM 0.5615 mL 2.8074 mL 5.6148 mL
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Research Update

Synthesis of L-glucose from D-Gulono-1,4-lactone

Carbohydr Res 1999 Sep 15;321(1-2):116-20.PMID:10612005DOI:10.1016/s0008-6215(99)00192-5.

An efficient method for the synthesis of L-glucose from D-Gulono-1,4-lactone via 1,2,3,4,5-penta-O-benzyl/acetyl/benzoyl-D-gulitol is described in 34-53% overall yield.

Characterisation of D-arabinono-1,4-lactone oxidase from Candida albicans ATCC 10231

Eur J Biochem 1994 Nov 1;225(3):1073-9.PMID:7957197DOI:10.1111/j.1432-1033.1994.1073b.x.

D-Erythroascorbic acid was detected from the cell extracts of a dimorphic fungus, Candida albicans. Its concentration in yeast cells grown at 25 degrees C was estimated to be about 0.45 mumol/ml cell water. D-Arabinono-1,4-lactone oxidase, which catalyses the final step in the biosynthesis of D-erythroascorbic acid, was purified 639-fold from the mitochondrial fraction of C. albicans to apparent homogeneity, with an overall yield of 21.2%, by a purification procedure consisting of Triton X-100 solubilisation, ammonium sulphate precipitation, anion-exchange, hydrophobic-interaction, gel-filtration and dye-ligand chromatographies. Gel-filtration chromatography and polyacrylamide-gradient gel electrophoresis in the presence of deoxycholate gave apparent molecular masses of 110 kDa and 84.4 kDa, respectively. SDS/PAGE showed only one protein band corresponding to a molecular mass of 66.7 kDa. Considering the binding of detergents, the enzyme is suggested to be a single polypeptide. The enzyme showed a typical fluorescence excitation spectrum of a flavin-containing enzyme. The flavin was not released by treatment with SDS, CCl3CO2H or boiling, indicating that it may be covalently bound to the enzyme protein. The enzyme was optimally active at 40 degrees C and at pH 6.1. The enzyme was stable in the range pH 7.5-10. An apparent Km value for D-arabinono-1,4-lactone was 44.1 mM. L-Galactono-1,4-lactone, L-gulono-1,4-lactone and L-xylono-1,4-lactone could also serve as substrates. Competitive inhibition was demonstrated with D-glucono-1,5-lactone, L-arabinono-1,4-lactone, D-galactono-1,4-lactone and D-Gulono-1,4-lactone. p-Chloromercuribenzoate, N-ethylmaleimide, iodoacetic acid, iodoacetamide and divalent metal ions such as Cd2+, Hg2+, Mn2+ and Zn2+ exhibited inhibitory effects on the enzyme.