| Literature DB >> 6244947 |
H G Mannherz, R S Goody, M Konrad, E Nowak.
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.Entities:
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Year: 1980 PMID: 6244947 DOI: 10.1111/j.1432-1033.1980.tb04437.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956