牛胰腺脱氧核糖核酸酶I与骨骼肌肌动蛋白的相互作用。

The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin.

作者信息

Mannherz H G, Goody R S, Konrad M, Nowak E

出版信息

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

DOI:10.1111/j.1432-1033.1980.tb04437.x

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.

摘要

当肌动蛋白与脱氧核糖核酸酶I复合时，肌动蛋白结合核苷酸的交换速率降低约20倍，而这并不影响钙与肌动蛋白的结合常数。已确定脱氧核糖核酸酶I与单体肌动蛋白和丝状肌动蛋白的结合常数分别为5×10⁸ M⁻¹和1.2×10⁴ M⁻¹。脱氧核糖核酸酶I引起的F-肌动蛋白解聚似乎是由于脱氧核糖核酸酶I使肌动蛋白的G-F平衡发生了改变。G-肌动蛋白对脱氧核糖核酸酶I的DNA降解活性的抑制属于部分竞争性类型。