The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin.
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.
D000199:Actins; D000255:Adenosine Triphosphate; D000818:Animals; D002417:Cattle; D004247:DNA; D003850:Deoxyribonuclease I; D003851:Deoxyribonucleases; D004720:Endonucleases; D007700:Kinetics; D046911:Macromolecular Substances; D009132:Muscles / Q000032:analysis*; D010179:Pancreas / Q000201:enzymology*; D010766:Phosphorylation; D011485:Protein Binding; D011817:Rabbits; D013050:Spectrometry, Fluorescence
D000199:Actins; D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D004247:DNA; D003851:Deoxyribonucleases; D004720:Endonucleases; D003850:Deoxyribonuclease I