The study demonstrates structural similarities between the Ca2+-dependent protein modulator of phosphodiesterase from bovine brain and muscle troponin C, suggesting conserved Ca2+-binding mechanisms.
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Structural similarity suggests conserved Ca2+ mechanisms; hypothesis-generating for phosphodiesterase regulation, no practice change.
Results of studies of the Ca2+-dependent protein modulator of 3':5'-cyclic nucleotide phosphodiesterase isolated from bovine brain are presented which show its structural similarity to the Ca2+-binding subunit of muscle troponin. Both proteins have blocked NH2 termini, similar and characteristic ultraviolet absorption spectra, similar Ca2+-binding properties, very similar amino acid compositions, and co-migrate on sodium dodecyl sulfate-polyacrylamide gels. The primary structures of selected tryptic peptides isolated from bovine brain modulator protein are similar or identical with regions of the primary sequences of rabbit skeletal muscle and bovine cardiac muscle troponin C. Bovine brain modulator protein contains and unidentified ninhydrin-positive basic compound not found in muscle troponin C. An improved procedure is presented which yields 40 to 70 mg of modulator protein per kg of bovine brain.
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Watterson et al. (1976) studied this question.
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