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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Revision of the structure for an endo-beta-N-acetylglucosaminidase H substrate using a novel modification of the Smith degradation.

(Man)5(GlcNAc)2Asn was shown in a previous study (Trimnble, R. B., Tarentino, A. L., Plummer, T. H., Jr., and Maley, F. (1978) J. Biol. Chem. 253, 4508-4511) to be hydrolyzed by alpha-mannosidase to Man alpha 1 leads to 6Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc beta 2 leads to 4GlcNAc-Asn. The latter is the most effective substrate for endo-beta-N-acetylglucosaminidase H tested to date. By employing a new and highly sensitive modification of the Smith degradation, it is shown that this compound is in reality Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man alpha 1 leads to 6Man beta 1 leads to 4GlcNAc beta 1eads to 4GlcNAc-Asn. The method entails the conversion of a glycosyl asparagine derivative to its corresponding dimethylaminonaphthyl sulfonyl analogue, which after periodate oxidation is treated directly with Dowex 50-H+ to eliminate the modified carbohydrate residues. The dansylated products, which are eluted from the resin with ammonium hydroxide, can be identified rapidly by thin layer chromatography.[1]

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