Binding of adenosine triphosphate to myosin

Schliselfeld, Louis H.; Bárány, Michael

doi:10.1021/bi00849a024

Cited by 60 publications

(32 citation statements)

References 23 publications

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“…For simplicity we can imagine that the attached dye exists either "firmly bound" (for a fraction of the time, f) or "loose" (for a fraction of the time, 1-A), and furthermore that when the dye is "loose" its angular velocity relative to its attachment adds to the angular velocity of S-1. Because of the proportionality of angular velocity to rotational diffusion coefficient the latter would be "Ds1i" [ ogy with thio-ATP (20), by a column method (21), and as a ratio of separately measured velocity constants (22). The AGO values generally lie between -6 and -7 kcal/mole.…”

Section: Theory Of the Methodsmentioning

confidence: 99%

Affinity of myosin S-1 for F-actin, measured by time-resolved fluorescence anisotropy.

Highsmith¹,

Mendelson²,

Morales³

1976

Proc. Natl. Acad. Sci. U.S.A.

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The association constant for myosin subfragment-1 (S-1) and actin was measured, using a new application of fluorescence depolarization which capitalizes on the fact that S-1 has high rotational mobility while F-actin does not. Uncoupling of the time dependences of the anisotropy decay and the association/dissociation phenomena allowed the experimentally determined anisotropy decay curve to be fitted by a sum of two terms weighted by the mole fractions of the free and bound S-1. At 4 degrees C, ionic strength 0.16 M, and pH 7.0, the association constant Ka is (1.73 +/- 0.35) X 10(6) M-1 at infinite dilution. This makes the -deltaG degrees of binding of F-actin to S-1 similar to the -deltaG degrees of binding of ATP to S-1, and the possible physiological relevance of the similarity to muscle contraction is discussed.

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Section: Theory Of the Methodsmentioning

confidence: 99%

Affinity of myosin S-1 for F-actin, measured by time-resolved fluorescence anisotropy.

Highsmith¹,

Mendelson²,

Morales³

1976

Proc. Natl. Acad. Sci. U.S.A.

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“…t Schliselfeld (1976). § In 25 mM-NaCI; Schliselfeld & Barany (1968). 1978 160 FROG MUSCLE MYOSIN, SUBFRAGMENT 1 AND ACTIN Table 3.…”

Section: Proteinmentioning

confidence: 99%

Preparation and characterization of frog muscle myosin subfragment 1 and actin

Ferenczi¹,

Homsher²,

Trentham³

et al. 1978

Biochemical Journal

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The preparation, structural and steady-state kinetic characteristics of contractile proteins from the leg muscle of frogs Rana temporaria and Rana pipiens are described. Actin and myosin from the two frog species are indistinguishable. The proteins have structural and steady-state kinetic properties similar to those from rabbit fast-twitch skeletal muscle. Chymotrypsin digestion of frog myosin or myofibrils in the presence of EDTA yields subfragment 1, which is separated by chromatography into two components that are distinguished by their alkali light-chain content.

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“…The precipitation of spin-labeled SI in the presence of MgADP was done in 60% saturated ammonium sulfate, 25 mM Tris-HCl, pH 8.0, and 4 mM MgADP. It was shown that myosin precipitated with ammonium sulfate in the presence of nucleotide contains a mole to mole ratio for nucleotide to myosin of -0.88 (Schliselfeld & Barany, 1968).…”

mentioning

confidence: 99%

Specificity and orientation of (iodoacetamido)proxyl spin-labeled myosin subfragment 1 decorating muscle fibers: localization of protein-bound spin labels using SDS-PAGE

Ajtai

Pótó

Burghardt³

1990

Biochemistry

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The nitroxide spin label (iodoacetamido)proxyl (IPSL) was specifically and rigidly attached to sulfhydryl 1 (SH1) on myosin subfragment 1 (S1). The specificity of this label for SH1 was demonstrated by using a technique where the spin label is localized on the electrophoresis-isolated proteolytic fragments of myosin using electron paramagnetic resonance (EPR). Studies of the rigidity of the probe on SH1 indicate that the IPSL is immobilized on the surface of S1 in the presence and absence of the nucleotides MgADP or MgATP. The EPR spectrum of muscle fibers decorated with IPSL-S1 shows that the IPSL-S1 rotates from its orientation in rigor upon binding MgADP. The angular displacement due to nucleotide binding is larger than that detected with the (maleimido)tempo spin label [Ajtai, K., French, A. R., & Burghardt, T. P. (1989) Biophys. J. 56, 535-541], demonstrating that the IPSL is oriented on the myosin cross-bridge in a manner that is favorable for detecting cross-bridge rotation during the rigor to MgADP state transition.

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Binding of adenosine triphosphate to myosin

Cited by 60 publications

References 23 publications

Affinity of myosin S-1 for F-actin, measured by time-resolved fluorescence anisotropy.

Affinity of myosin S-1 for F-actin, measured by time-resolved fluorescence anisotropy.

Preparation and characterization of frog muscle myosin subfragment 1 and actin

Specificity and orientation of (iodoacetamido)proxyl spin-labeled myosin subfragment 1 decorating muscle fibers: localization of protein-bound spin labels using SDS-PAGE

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