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Preparation, characterization, and properties of a novel triple-modified derivative of the Ca2+ -dependent protein modulator.

A novel, chemically modified derivative of the Ca2+-dependent protein modulator of cyclic nucleotide phosphodiesterase was prepared by the sequential treatment of the native protein with tetranitromethane, 1,2-cyclohexanedione, and diethylpyrocarbonate. Three derivatives were isolated during the synthesis, i.e., a single-modified derivative containing two modified tyrosine residues per mole; a double-modified derivative containing two modified tyrosines plus five modified arginine residues per mole; and a triple-modified derivative containing two modified tyrosines, five modified arginines, and one modified histidine residue per mole. Intermolecular cross-linking was observed to occur as a minor side reaction during nitration of the native protein with tetranitromethane. All the derivatives were examined for phosphodiesterase-stimulating activity and troponin C like activities. All derivatives were found to retain the capacity of the native protein to stimulate modulator-deficient phosphodiesterase; furth...