English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse
  1. View item / 
  2. Item Summary

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin

MPS-Authors
/persons/resource/persons122112

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;

/persons/resource/persons98693

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;

External Resource

https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/j.1432-1033.1980.tb04437.x
(Any fulltext)

https://doi.org/10.1111/j.1432-1033.1980.tb04437.x
(Any fulltext)

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
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: https://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.