NAD+ glycohydrolase, an ecto-enzyme of calf spleen cells

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Abstract
A sensitive fluorometric assay of NAD glycohydrolase was used to show that calf spleen cells are able to hydrolyse 1,N6-etheno-NAD given in the medium. The observed rates of substrate hydrolysis and product accumulation in the medium are equivalent. Moreover, the splenocytes are able to cleave the nicotinamide-ribose bond of a water-soluble polymer of NAD, and their NAD glycohydrolase activity is fully inhibited by a high-MW Blue Dextran. Selective permeation of the cellular membrane digitonin revealed an intracellular pool of NAD glycohydrolase, which accounts for 25% of the total activity. NAD glycohydrolase associated with the splenocytes has the characteristics of an ectoenzyme.