1972
DOI: 10.1021/bi00775a003
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Binding of actin to heavy meromyosin in the absence of adenosine triphosphate

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1973
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Cited by 41 publications
(28 citation statements)
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“…Similar effect of 3 mM MgATP on the H-meromyosin -actin system, a dissociation of the complex by about 60 %, has recently been observed by Eisenberg et al [45]. More work seems to be needed to decide if this phenomenon reflects a change in state of myosin, as suggested by these authors, or in actin.…”
Section: Resultssupporting
confidence: 77%
See 1 more Smart Citation
“…Similar effect of 3 mM MgATP on the H-meromyosin -actin system, a dissociation of the complex by about 60 %, has recently been observed by Eisenberg et al [45]. More work seems to be needed to decide if this phenomenon reflects a change in state of myosin, as suggested by these authors, or in actin.…”
Section: Resultssupporting
confidence: 77%
“…As pointed out by Eisenberg et al [45], some relationship might be indicated by the results of X-ray diffraction studies on living muscle suggesting that only a fraction of the myosin heads bind to actin filaments during contraction [48,49].…”
Section: Resultsmentioning
confidence: 92%
“…F-Actin was prepared as in [17]. S-I and F-actin were labeled with N-(iodoacetyl)-N' -(5-sulfo-1-naphthyl)ethylenediamine (1,5-IAEDANS) according to [2].…”
Section: Methodsmentioning
confidence: 99%
“…Actin was prepared from rabbit skeletal muscle [14,15] and isolated as G-actin (50-60 FM) by a final chromatography step using Sephadex G-200 in buffer G (5 mM Tris-Cl, pH 7.8, 0.2 mM dithiothreitol, 0.1 mM CaCl2, 0.2 mM ATP, 0.01% NaN3). Ca-G-actin was converted to Mg-G-actin by incubation for 3 min at 20°C in the presence of buffer G containing 0.2 mM EGTA and 50 PM MgClz.…”
Section: Actinmentioning
confidence: 99%