Results 161 to 170 of about 2,484 (223)

Skeletal muscle myosin subfragment 1 dimers

Biophysical Chemistry, 1997
The rate of translational diffusion of skeletal muscle myosin subfragment 1 (S1) was determined from polarized dynamic light scattering autocorrelation measurements. Diffusion rates were expressed in terms of the hydrodynamic radii Rh. At 20 degrees C, in low ionic strength pH 8 solutions, Rh increased from 4.3 nm to 5.7 nm as [S1] was increased from 1.
K, Claire, R, Pecora, S, Highsmith
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Photocleavage of myosin subfragment 1 by vanadate

Biochemistry, 1990
The heavy chain of myosin's subfragment 1 (S1) was cleaved at two distinct sites (termed V1 and V2) after irradiation with UV light in the presence of millimolar concentrations of vanadate and in the absence of nucleotides or divalent metals. The V1 site cleavage appeared to be identical with the previously described active site cleavage at serine-180,
C R, Cremo, G T, Long, J C, Grammer
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Interaction of globular actin with myosin subfragments

Journal of Molecular Biology, 1971
Abstract We have attached a spin label or a fluorescent dye to actin to probe the interaction of G-actin with myosin subfragments. The spin label spectra, which are sensitive to the polymerization of the actin, showed that when heavy meromyosin was added to G-actin the actin was polymerized.
R, Cooke, M F, Morales
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The interdomain motions in myosin subfragment 1

Biophysical Chemistry, 2001
The interdomain motions in myosin subfragment 1 (S1) were studied by steady-state and time-resolved fluorescence of tryptophan residues and N-(iodoacetyl)-N'-(5-sulfo-1-naphtyl)ethylenediamine (AEDANS) attached to Cys178 of alkali light chain 1 (A1) exchanged into S1.
Y K, Reshetnyak, O A, Andreev
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Homogeneity of myosin subfragments by equilibrium centrifugation

Biochemistry, 1981
A number of enzymes are currently in use for obtaining proteolytic subfragments of rabbit skeletal muscle myosin. Subfragment-1 can be obtained by papain digestion of polymeric myosin in the presence (Mg-S1) or absence (EDTA-S1) of divalent cations [Margossian, S.S., Lowey, S., & Barshop, B. (1975) Nature (London) 258, 163-166].
S S, Margossian, W F, Stafford, S, Lowey
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Structural stability of fish myosin subfragment-1

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1990
1. Tryptic cleavage of fish myosin subfragment-1 (S-1) revealed its similar substructure of heavy chain to that of rabbit S-1. 2. The structural stability of fish S-1 was studied by thermal denaturation method, and a rapid polymerization of inactivated fish S-1, detected by turbidity increase, was characteristic. 3.
M, Hamai, K, Konno
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Fluorescence energy transfer in myosin subfragment-1

Biochemistry, 1980
Fluorescent probes have been selectively introduced into skeletal muscle myosin subfragment-1 and the fluorescence emission characteristics of the labeled products studied. The fluorophores employed were the thiol-specific reagents N-[[(iodoacetyl)aminolethyl-5-naphthylamine-1-sulfonic acid and 5-(iodoacetamido)fluorescein, the spectral properties of ...
D J, Marsh, S, Lowey
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Myosin subfragment 1 has tertiary structural domains

Biochemistry, 1986
Transient electrical birefringence measurements were made on skeletal muscle myosin subfragment 1 (S1) at 3.7 degrees C in 10 mM tris(hydroxymethyl)aminomethane-acetate and 0.10 mM MgCl2, pH 7.0. The specific birefringence for 4.5 microM S1 was determined from steady-state measurements to be (8.1 +/- 0.3) X 10(-7) (cm/statvolt)2. For electric fields in
S, Highsmith, D, Eden
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Interaction of myosin subfragments with F-actin

Biochemistry, 1978
The effect of ionic strength, temperature, and divalent cations on the association of myosin with actin was determined in the ultracentrifuge using scanning absorption optics. The association constant (Ka) for the binding of heavy meromyosin (HmM) to F-actin was 1 X 10(7) M-1 at 20 degrees C, in 0.10 M KCl, 0.01 M imidazole (pH 7.0), 5 MM potassium ...
S S, Margossian, S, Lowey
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Binding of Myosin Subfragment 1 to Actin

Journal of Biochemistry, 1996
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 approximately 100- and approximately 100,000-fold in the ...
T, Katoh, F, Morita
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