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methyl 2-O-acetyl-3,4-di-O-benzyl-β-D-fucopyranoside is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

96048-29-2

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96048-29-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 96048-29-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,6,0,4 and 8 respectively; the second part has 2 digits, 2 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 96048-29:
(7*9)+(6*6)+(5*0)+(4*4)+(3*8)+(2*2)+(1*9)=152
152 % 10 = 2
So 96048-29-2 is a valid CAS Registry Number.

96048-29-2Relevant academic research and scientific papers

Synthesis and unusual glycosidic coupling reaction of substituted 2,7-dioxabicycloheptanes: 1,2-anhydro-3,4-di-O-benzyl-α-D-fucopyranose

Du, Yuguo,Kong, Fanzuo

, p. 413 - 420 (2007/10/03)

Keywords: 2,7-Dioxabicycloheptanes; Synthesis; Glycosidic coupling reaction

Synthesis of Some Disaccharides Containing an L-Rhamnopyranosyl or L-Mannopyranosyl Residue, and the Substrate-specificity of α-L-Rhamnosidase from Aspergillus niger

Kamiya, Shintaro,Esaki, Sachiko,Tanaka, Reiko

, p. 55 - 62 (2007/10/02)

In order to investigate the substrate-specificity of α-L-rhamnosidase from Aspergillus niger, the following disaccharides were synthesized: 2-O-α-L-rhamnopyranosyl-α-D-fucopyranose (1), methyl 4-O-α-L-rhamnopyranosyl-β-L-arabinopyranoside (2), methyl 2-O-α-L-rhamnopyranosyl-α-L-rhamnopyranoside (3) and 6-O-α-L-mannopyranosyl-D-glucopyranose (4).The action of α-L-rhamnosidase on compounds 1 - 4 and another fifteen disaccharides containing α- or β-L-rhamnopyranosidic bonds or an α-L-mannopyranosidic bond was examined.As the result, all the disaccharides having an α-L-rhamnopyranosidic linkage were hydrolyzed well, while the ones having β-L-rhamnopyranosidic or α-L-mannopyranosidic linkage could not be hydrolyzed at all.Accordingly, this enzyme might be used for the determination of anomeric configurations of the L-rhamnopyranosidic bond, although further studies on the specificity of the enzyme are required.

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