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应用
Endoglycoceramidase II from Rhodococcus sp. has been used in a study to assess the differentiation of glycosphingolipid-derived glycan structural isomers by liquid chromatography and mass spectrometry. Endoglycoceramidase II from Rhodococcus sp. has also been used in a study to investigate structural and mechanistic analyses of endo-glycoceramidase II.
单位定义
One unit will hydrolyze 1 μmol of asialo-GM1 per min at 37 °C at pH 5.0.
外形
Solution in 20 mM sodium acetate buffer, pH 6.0, containing 0.2% BSA and 0.1% Lubrol PX.
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
新产品
Glycobiology, 20(9), 1103-1116 (2010-05-15)
Isolation and characterization of glycosphingolipids is of importance in many aspects of glycobiology, but is difficult to achieve due to the high degree of heterogeneity and isomerism present in these compounds. In this study, oligosaccharides obtained from non-acid glycosphingolipids by
The Journal of biological chemistry, 280(42), 35164-35171 (2005-08-24)
Clostridium botulinum neurotoxins (BoNTs) act on nerve endings to block acetylcholine release. Their potency is due to their enzymatic activity and selective high affinity binding to neurons. Although there are many pieces of data available on the receptor for BoNT
Journal of biochemistry, 142(2), 239-246 (2007-06-15)
Endoglycoceramidase is a glycohydrolase capable of hydrolysing the O-glycosidic linkage between oligosaccharides and ceramides of various glycosphingolipids. However, no endoglycoceramidase reported so far can hydrolyse 6-gala series glycosphingolipids which possess the common structure R-Gal beta1-6Gal beta1-1'Cer. Recently, we found a
The Journal of biological chemistry, 282(15), 11386-11396 (2007-01-25)
Enzymes capable of hydrolyzing the beta-glycosidic linkage between oligosaccharides and ceramides in various glycosphingolipids has been found in microorganisms and invertebrates and designated endoglycoceramidase (EC 3.2.1.123) or ceramide glycanase. Here we report the molecular cloning, characterization, and homology modeling of
Journal of biochemistry, 130(2), 263-268 (2001-08-02)
Endoglycoceramidase (EGCase: EC 3.2.1.123) is an enzyme capable of cleaving the glycosidic linkage between oligosaccharides and ceramides in various glycosphingolipids. We report here transglycosylation and reverse hydrolysis reactions of EGCase from the jellyfish Cynaea nozakii. Various alkyl-GM1 oligosaccharides (alkyl-II(3)NeuAcGgOse4) were
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