Results 201 to 210 of about 2,706 (221)

A new method for producing myosin subfragment-1

Biochemical and Biophysical Research Communications, 1972
Abstract Myosin subfragment-1 (S1) was produced from myosin by digestion with papain while the myosin was “in situ” in a muscle fibril. S1 was extracted from the fibrils using Mg-PP i , and chromatographed on Sephadex G-200. This S1 had sedimentation and diffusion coefficients similar to those found for S1 by previous workers.
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Interaction of Myosin Subfragment 1 with Forms of Monomeric Actin

Biochemistry, 2003
The ability of myosin subfragment 1 to interact with monomeric actin complexed to sequestering proteins was tested by a number of different techniques such as affinity absorption, chemical cross-linking, fluorescence titration, and competition procedures. For affinity absorption, actin was attached to agarose immobilized DNase I.
Ballweber, E., Kiessling, P., Manstein, D., Mannherz, H.   +3 more
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Differential scanning calorimetry of the unfolding of myosin subfragment 1, subfragment 2, and heavy meromyosin

Biochemistry, 1990
The thermal unfolding of rabbit skeletal heavy meromyosin (HMM), myosin subfragment 1, and subfragment 2 has been studied by differential scanning calorimetry (DSC). Two distinct endotherms are observed in the DSC scan of heavy meromyosin. The first endotherm, with a Tm of 41 degrees C at pH 7.9 in 0.1 M KCl, is assigned to the unfolding of the ...
John W. Shriver, Utpala Kamath
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The interaction of skeletal myosin subfragment 1 with the polyanion, heparin

European Journal of Biochemistry, 1984
The association between chymotryptic skeletal muscle myosin subfragment 1 (S1) and the polyanion, heparin, was investigated as an experimental approach in probing the functional importance of the cationic sites on S1 and their involvement in ionic interactions within the myosin head during energy transduction.
Etienne Audemard, Raoul Bertrand, Ridha Kassab, Jean-Pierre Labbé, D Walzthöny, Theo Wallimann   +5 more
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Interactions of myosin subfragment 1 isozymes with G-actin

Biochemistry, 1991
The polymerization of G-actin by myosin subfragment 1 (S-1) isozymes, S-1(A1) and S-1(A2), and their proteolytically cleaved forms was studied by light-scattering, fluorescence, and analytical ultracentrifugation techniques. As reported previously, S-1(A1) polymerized G-actin rapidly while S-1(A2) could hardly promote the assembly reaction (Chaussepied
Emil Reisler, Theresa Chen
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Preparation of the Enzymatically Active Subfragment of Myosin by Proteolysis of Myofibrils

European Journal of Biochemistry, 1973
Myofibrils, when submitted to proteolysis, yield several fragments, some of which remain bound to actin. There are separated by pyrophosphate treatment and isolated by preparative centrifugation. When trypsin treatment is performed in the presence of 1 mM CaCl2, two types of products are obtained, which can be separated by chromatography on DEAE ...
Elisabeth Ehrilich, Endre N. A. Biro, Rose Coelho, Christiane Dvonc, Florent Guillain   +4 more
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o-Iodosobenzoic oxidation and cleavage of myosin subfragment 1

International Journal of Biochemistry, 1992
1. o-Iodosobenzoic acid (IOB) caused the formation of a disulfide bridge between SH1 and SH2 groups of myosin SF1 rendering inactive its ATPase activity. 2. IOB at high concentrations provoked fragmentation of SF1 at its tryptophan residues. 3. The main fragmentation point was located at 15 K from the amino terminus of the myosin heavy chain. 4.
Natalia López-Moratalla, Belén Garrido, Guillermo Zalba, Esteban Santiago, Carlos Longo   +4 more
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Ionization of reactive lysyl residue of myosin subfragment 1

Biochemistry, 1981
The epsilon-NH2 groups of lysyl residues of myosin subfragment 1 belong to two classes on the basis of their reaction with 2,4,6-trinitrobenzenesulfonate: on reactive lysyl residue and 82 slow-reacting lysyl residues. The trinitrophenylation of the reactive lysyl residue is accompanied by a sharp decrease in the K+(EDTA)-activated ATPase of myosin ...
Andras Muhlrad, Reiji Takashi
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Interaction of monomeric and polymeric actin with myosin subfragment 1

Journal of Molecular Biology, 1972
Abstract The abilities of F-actin and G-actin to activate the ATPase of subfragment 1 of myosin have been compared at 15 °C in a medium of low ionic strength in which polymerization of G-actin does not occur. F-actin gives a very much larger activation than G-actin, but the activation by G-actin is still appreciable. At 25 °C the difference between G-
Gerald Offer, Lesley Baker, Harry F. Baker   +2 more
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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
Don Eden, Stefan Highsmith
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