caa a22 4500 397557272 CHVBK 20180308164806.0 cr unu---uuuuu 161202e199607 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021384 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021384 Binding of Myosin Subfragment 1 to Actin [Elektronische Daten] [Tsuyoshi Katoh, Fumi Morita] The dissociation constant for the binding of myosin subfragment 1 (S1) and chromatographed actin in the presence and absence of nucleotide was measured at various ionic strengths and various temperatures. The dissociation constant was of nM order in the absence of nucleotide and increased by ∼100- and ∼100,000-fold in the presence of ADP and ATP, respectively. The dissociation constant also increased with increasing ionic strength, irrespective of the presence of nucleotide, and its dependence on the ionic strength was increased by the presence of ATP but decreased by the presence of ADP. The standard enthalpy change and entropy change for the binding of S1 to actin were both positive, irrespective of the presence of nucleotide, indicating that the binding was entropy-driven. The standard entropy change was essentially unaffected by the presence of ADP but was greatly decreased by ATP, suggesting that the large increase in the dissociation constant in the presence of ATP was due to the decrease of hydrophobic Interactions. On the other hand, the increase in the dissociation constant for acto-S1 in the presence of ADP might be induced by the decrease of electrostatic interactions. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence actin nationallicence actomyosin nationallicence actomyosin ATPase nationallicence acto-S1 nationallicence myosin nationallicence Katoh Tsuyoshi Division of Chemistry Graduate School of Science, Hokkaido University, Kita-ku, Sapporo 060 aut Morita Fumi Division of Chemistry Graduate School of Science, Hokkaido University, Kita-ku, Sapporo 060 aut The Journal of Biochemistry Oxford University Press 120/1(1996-07), 189-192 0021-924X 120:1<189 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021384 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021384 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Katoh Tsuyoshi Division of Chemistry Graduate School of Science, Hokkaido University, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Morita Fumi Division of Chemistry Graduate School of Science, Hokkaido University, Kita-ku, Sapporo 060 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/1(1996-07), 189-192 0021-924X 120:1<189 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford