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The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin

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Mannherz,  Hans Georg
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Goody,  Roger S.
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Abt. III: Strukturbiochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Mannherz, H. G., Goody, R. S., Konrad, M., & Nowak, E. (1980). The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin. European Journal of Biochemistry, 104(2), 367-379. doi:10.1111/j.1432-1033.1980.tb04437.x.


Cite as: http://hdl.handle.net/21.11116/0000-0004-B6C1-4
Abstract
The rate of exchange of actin-bound nucleotide is decreased by a factor of about 20 when actin is complexed with DNAase I without affecting the binding constant of calcium for actin. Binding constants of DNAase I to monomeric and filamentous actin were determined to be 5 X 10(8) M-1 and 1.2 X 10(4) M-1 respectively. The depolymerisation of F-actin by DNAase I appears to be due to a shift in the G-F equilibrium of actin by DNAase I. Inhibition of the DNA-degrading activity of DNAase I by G-actin is of the partially competitive type.