PMID: 6108950Jan 10, 1981Paper

Ca2+-dependent modulator proteins from Tetrahymena pyriformis, sea anemone, and scallop and guanylate cyclase activation.

The Journal of Biological Chemistry
S KakiuchiK Yagi

Abstract

Previously, the guanylate cyclase activity of Tetrahymena pyriformis was shown to be activated by an endogenous modulator (calmodulin)-like protein (Na-gao, S., Suzuki, Y., Watanabe, Y., and Nozawa, Y. (1979) Biochem. Biophys. Res. Commun. 90, 261-268). This protein has now been identified as the modulator protein. The identification was based on the capability of this protein to activate the brain modulator-deficient phosphodiesterase and the mobility of this protein upon polyacrylamide gel electrophoresis. The activation of guanylate cyclase was specifically attributable to the Tetrahymena modulator protein since other modulator proteins examined (bovine brain, sea anemone, and scallop) were ineffective. Under the conditions where the activation of Tetrahymena guanylate cyclase occurred, guanylate cyclase activities from other sources, that include rat brain, rat lung, and human platelet, were not affected. In the phosphodiesterase activation, the potencies of scallop and Tetrahymena modulator proteins, which are represented by reciprocals of the quantities of proteins required for half-maximal activation of enzyme, were 66% and 55%, respectively, of that of the brain protein. The same decreasing order was seen for the affini...Continue Reading

Related Concepts

Related Feeds

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.