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Intrigued by similar specificities of the hydra feeding receptor and γ-glutamyl transferase activity toward GSH, we examined the possibility that these two GSH-bihding activities might reside in the same protein. We find that the two activities differ in specificity toward the γ-glutamyl moiety of GSH. The hydra transferase recognizes L-azaserine, L-Glu, D-Glu and L-Gln. The feeding receptor recognizes only L-GlU and L-Gln; L-azaserine and D-Glu have no effect. L-azaserine, known to bind covalently to the γ-glutamyl donor site of mammalian transferase, irreversibly inactivates hydra transferase activity. The transferase affinity label, however, has no effect on the GSH-stimulated feeding response, permitting us to demonstrate that these two activities have different GSH recognition sites and appear to reside in different proteins. Note:

Azaserine Affinity Labelling of γ-Glutamyl Transferase of Hydra Attenuata Without Inactivation of the Glutathione Receptor