Aglycone and Natural Glycosidic Binding Partners

Recent studies have implicated the existence of a hydrophobic centre distinct from the catalytic centre in V. cholerae (Keilich et al. 1979) and C. perfringens (Corfield et al. 1980) sialidases. The detection of multiple sialidase activities in bacterial, protozoan and mammalian sialidase preparations using immobilized N-(4-nitrophenyl)-oxamic acid columns has supported these observations (Brossmer et al. 1977 b, Crampen et al 1979, Ziegler et al 1980). Those sialidases showing affinity for the immobilized ligand also showed low activity with synthetic 

It is important to realize that a(2-3), (2-6), and (2-8) linkages occur in all complex carbohydrate classes, and may be combined within one molecule in some cases (see chapter B, Strecker and Montreuil 1979, Corfield et al. 1981 a), and that the specificity outlined above also relates to the different classes of complex 

Clostridium perfringens Vibrio cholerae Arthrobacter ureafaciens Newcastle disease virus Influenza A2 virus Fowl plague virus Rat liver Golgi Human liver lysosomal Human fibroblast 

New studies have expanded the work of Drzeniek (1972, 1973) with regard to the glycosidic linkage specificity of viral and bacterial sialidases (Corfield et al. 1981 a, b), allowing discrimination between three different viral sialidase activities on the basis of a(2-3) and (2-6) linkages and the nature of the oligosaccharide chain in substrates as described under IV. 3.g). 

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