Preparation and Properties of Catalytically Active Endosialidase

coli K1 specific bacteriophages have been tested for phage-typing of bacterial strains [152], but this application has not found much use. It was somi discovered that the bacteriophage-derived endosialidase is suitable for the study of eukaryotic 

The pH optimum of endoNE has been reported to be sfightly above 5 [101]. Using a TFMU sialotrioside substrate (TEMU a-Unked trifluoromethylumbelUferyl glycoside) and monitoring the release of the free coumarin endoNF has been fotmd to have a pH optimum around 4.5 [127]. Determination of at a series of pH values has 

Acetate is preferred over phosphate as the buffer anion, and the catalytic activity is reduced in the presence of 9 mM Ca [101]. However, it should be noted that endosialidase is still active under physiological conditions in the presence of phosphate and calcium. Polyanions, like DNA, have been reported to inhibit the activity of endoNF [104]. 

The active endosialidase with its ability to specifically degrade polysialic acid represents a powerful tool for the study of the chemistry, metabolism, and biological roles of polysialic acid. The inactive endosialidase, on the other hand, able to recognize specifically and remain botmd to polysialic acid, represents a sensitive and convenient tool for the specific detection of polysialic in different applications. 

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