Add time:08/14/2019         Source:sciencedirect.com

Publisher SummaryCyclic ADP-ribose (cADPR) is a Ca2+-mobilizing cyclic nucleotide that functions as an endogenous modulator of the Ca2+-induced Ca2+ release mechanism in cells. Its synthesizing enzyme, ADP-RIBOSYLCYCLASE (cas 135622-82-1), is widely distributed among animal tissues and is particularly abundant in Aplysia ovotestis. This chapter describes a procedure for a one-step large-scale purification of the Aplysia cyclase that is useful for biochemical analyses and crystallography. A lymphocyte antigen, CD38, which shares considerable sequence homology with the Aplysia cyclase, is shown to possess not only the cyclase activity but also to catalyze the hydrolysis of cADPR. A fluorimetric assay based on using nicotinamide guanine dinucleotide (NGD+), a guanine analog of NAD+, is proposed in the chapter. NGD is cyclized by CD38 to produce cyclic GDP-ribose (cGDPR), which is fluorescent. The product is also resistant to hydrolysis and accumulates, making this simple fluorimetric assay ideally suitable for monitoring the cyclize activity of CD38-like bifunctional enzymes in crude tissue extracts and during purification.

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