The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin

Eur J Biochem. 1980 Mar;104(2):367-79. doi: 10.1111/j.1432-1033.1980.tb04437.x.


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.

MeSH terms

  • Actins*
  • Adenosine Triphosphate
  • Animals
  • Cattle
  • DNA
  • Deoxyribonuclease I
  • Deoxyribonucleases*
  • Endonucleases*
  • Kinetics
  • Macromolecular Substances
  • Muscles / analysis*
  • Pancreas / enzymology*
  • Phosphorylation
  • Protein Binding
  • Rabbits
  • Spectrometry, Fluorescence


  • Actins
  • Macromolecular Substances
  • Adenosine Triphosphate
  • DNA
  • Deoxyribonucleases
  • Endonucleases
  • Deoxyribonuclease I