Abstract

Covalent modification of arginine residues with phenylglyoxal and lysine residues with 4,4′-diisothiocyano-2,2′-disulphonic acid stilbene (DIDS) was carried out in preparations of rat cerebellar microsomes, as was the interaction of silver ions (silver nitrate) with cysteine residues. The effects of these amino acid-reactive agents on [ 3H]inositol 1,4,5-triphosphate (InsP 3) binding and InsP 3-induced calcium release were assessed. Both phenylglyoxal and DIDS inhibited [ 3H]InsP 3 binding and InsP 3-induced calcium release (IC 50 = 2.0 mM and 18 μM, respectively). Silver ions inhibited InsP 3-induced Ca 2+ release alone (IC ≈ 1 μM). These results suggest that arginine and lysine residues may be located at or close to the InsP 3 binding site of the InsP 3 receptor, while cysteine residues are important in channel opening.

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