Abstract
Phosphorylation of the TNT subunit of troponin (molecular weight 39,000) and a component of molecular weight 45,000 contained in actin has been carried out with phosphorylase kinase and a 3′5′-cAMP dependent protein kinase respectively. Upon phosphorylation of the latter protein calcium sensitivity of the reconstituted actomyosin ATPase is increased 2 to 4 fold. The 45,000 molecular weight fraction can be separated from crude G-actin by gel filtration over Sephadex G-200 and sedimentation of the repolymerized F-actin. The 45,000 molecular weight component remains in the supernatant and following phosphorylation with 3′5′-cAMP dependent protein kinase the material has been characterized by electrophoresis in SDS and urea.
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Abbreviations
- SDS:
-
sodium dodecylsulfate
- EGTA:
-
ethyleneglycol-bis-(β-amino-ethylether) N-N′-tetraacetic acid
- 3′5′-cAMP:
-
cyclic 3′5′-adenos-nemonophosphate
References
Bergmeyer, H. U., and Bernt, E., (1970), Methoden der enzymat., Analyse I., Bergmeyer, H.U. ( ed ), Verlag Chemie, p. 533.
Bowman, W. C., and Nott, M. W., (1969), Pharmacological Reviews, 21, 27.
Drabikowski, W., Nowak, E., Barylko, B., and Dabrowska, R., (1972), Cold Spring Harbor Symposia on Quantitative Biology, 37, 245.
Ebashi, S., Endo, M., and Ohtuski, I., (1969), Quarterly Reviews of Biophysics, 2, 351.
Ebashi, S., Ohtsuki, I., and Mihashi, K., (1972), Cold Spring Harbor Symposia on Quantitative Biology, 37, 215.
Ebashi, S., Wakabayashi, T., and Ebashi, F., (1971), J. Biochem., 69, 441.
Ellis, S., and Beckett, S. B., (1954), J. Pharmacol. Exp. Thr., 112, 202.
England, P. J., Stull, J. T., and Krebs, E. G., (1972), J. BioZ. Chem., 247, 5275.
Fiske, C. H., and Subba-Row, Y., (1925), J. Biol. Chem., 66, 375.
Glynn, T. M., and Chappell, J. B., (1964), Biochem. J., 90, 147.
Greaser, M. L., Yamaguchi, M., Brekke, C., Potter, J., and Gergely, J., (1972), Cold Spring Harbor Symposia on Quantitative Biology, 37, 235.
Haschke, R. H., and Heilmeyer, L. M.G., Jr.,(1972), Anal. Biochemistry, 47, 451.
Hartshorne, D. J., Perry, S. V., and Schaub, M. C.,(1967), Biochem. J., 104, 907.
Hartshorne, D. J., and Müller, H., (1969), Biochim. Biophys. Acta, 175, 301.
Hartshorne, D. J., and Dreizen, P., (1972), Cold Spring Harbor Symposia on Quantitative Biology, 37, 225.
Jennissen, H. P., and Heilmeyer, L. M. G Jr,,(1973),Anal. Biochem., in preparation.
Krebs, E. G., (1972), Current Topics in Cellular Regulation, 5, 99.
Krebs, E. G,, Reimann, E. M. and Walsh, D. A., (1971), J. Biol. Chem., 246, 1986.
Kuehl, W. M., and Adelstein, R. S., (1970), Biochem. Biophys. Res. Comm., 39, 956.
Lowry, O., (1951), J. Biol. Chem., 193, 265.
Nauss, K. M., Kitagawa, S., and Gergely, J., (1969), J. Biol. Chem., 244, 755.
Perrie, W. T., Smillie, L. B., and Perry, S. V., (1972), Cold Spring Harbor Symposia on Quantitative Biology, 37, 17.
Perry, S. V., and Grey, T. C., (1956), Biochem. J., 64, 184.
Perry, S. V., and Cole, H. A., (1973), Biochem. J., 131, 425.
Portzehl, H., Caldwell, P. C., and Rüegg, J. C., (1964), Biochim. Biophys. Acta, 79, 581.
Pratje, E., and Heilmeyer, L. M. G., Jr., (1972), FEES Letters, 27, 89.
Rees, M. K., and Young, M., (1967), J. Biol. Chem., 242, 4449.
Schaub, M. C., and Perry, S. V., (1969), Biochem, J., 115, 993.
Schaub, M. C., and Perry, S. V., (1971), Biochem. J., 123, 367.
Small, P. A., Harrington, W. P., and Kielley, W. W., (1961), Biochim. Biophys. Acta, 49, 462.
Staprans, I., Takahashi, H., Russell, M. P., and Watanabe, S., (1972), J. Biochem., 72, 723.
Stull, J. T., Brostrom, C. O., and Krebs, E. G., (1972), J. Biol. Chem., 247, 5272.
Taylor, E. W., (1972), Ann. Rev, of Biochemistry, 41, 577.
Weber, K., and Osborne, M., (1969), J. Biol. Chem., 244, 4406.
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Pratje, E., Heilmeyer, L.M.G. (1974). The Effect of Phosphorylation of Structural Muscle Proteins on the Actomyosin ATPase. In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_18
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DOI: https://doi.org/10.1007/978-3-642-80817-3_18
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