Results 171 to 180 of about 2,484 (223)
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Thermal Gelation Characteristics of Myosin Subfragments
Journal of Food Science, 1990ABSTRACT To elucidate the roles of the head and the tail portions of the molecule in the thermal gelation of myosin, the gelation characteristics of heavy meromyosin (HMM) and of light meromyosin (LMM) were investigated. The aggregation process of HMM corresponded to that of myosin alone in the temperature range above 50°C.
TAKESHI SANO +3 more
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Ligand-induced myosin subfragment 1 global conformational change
Biochemistry, 1990The effects of selected ligands on the structure of myosin subfragment 1 (S1) were compared by using transient electrical birefringence techniques. With pairs of dilute solutions of S1 at 3.5 degrees C in low ionic strength (mu = 0.020 M) buffers that had matched electrical impedances, S1 with Mg2+, MgADP, or MgADP.Vi bound was subjected to 6-7 ...
S, Highsmith, D, Eden
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Thermophysical Characterization of Tilapia Myosin and Its Subfragments
Journal of Food Science, 2011Abstract: Purified tilapia myosin was digested with α‐chymotrypsin and purified to obtain heavy meromyosin (HMM) and light meromyosin (LMM). The thermophysical properties of Tilapia myosin, HMM, and LMM were characterized.
Zachary H, Reed, Jae W, Park
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Incorporation of 6-carboxyfluorescein into myosin subfragment 1
Biochemistry, 1985We describe for the first time the introduction of a label into the "50K" domain of myosin subfragment 1 (S-1), and we investigate the properties of this fluorescent modification in relation to the ATPase and actin-binding activities, both residing in the myosin head. The labeling consists of a major incorporation of 6-carboxyfluorescein into the "50K"
D, Mornet, K, Ue
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Proteolytic separation of an enzymic active subfragment from the myosin-subfragment (S-1)
Biochemical and Biophysical Research Communications, 1967Abstract Direct visualization of myosin molecule by electron microscopy has shown it to be a long rod with a globular head at one end (Rice 1961 Huxley 1963). The use of proteolytic enzymes such as trypsin and chymotrypsin can cleave myosin into well defined and high molecular weight fragments, heavy and light meromyosins (Szent-Gyorgyi 1953 Gergely ...
K, Yagi, Y, Yazawa, T, Yasui
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Kinetic characterization of reductively methylated myosin subfragment 1
Biochemistry, 1993Reductive methylation of myosin-S1 converts 97% of lysine residues in native myosin-S1 to dimethyllysine without detectable modification of other amino acid side chains. RM-S1 is catalytically active, although the rate and equilibrium constants of many of the steps of the actomyosin ATP hydrolysis mechanism have been altered.
H D, White, I, Rayment
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Binding of myosin subfragment-1 to F-actin
Biochemical and Biophysical Research Communications, 1992During a part of the hydrolytic cycle, myosin head (S1) carries no nucleotide and binds strongly to an actin filament forming a rigor bond. At saturating concentration of S1 in rigor, S1 is well known to form 1:1 complex with actin. However, we have provided evidence that under certain conditions S1 could also form a complex with 2 actin monomers in a ...
O, Andreev, J, Borejdo
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o-Iodosobenzoic oxidation and cleavage of myosin subfragment 1
International Journal of Biochemistry, 19921. 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.
C, Longo +4 more
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Bundling of myosin subfragment-1-decorated actin filaments
Journal of Molecular Biology, 1987We have reported previously that rabbit skeletal myosin subfragment-1 (S-1) assembles actin filaments into bundles. The rate of this reaction can be estimated roughly from the initial rate (Vo) of the accompanying turbidity increase ("super-opalescence") of the acto-S-1 solution. Vo is a function of the molar ratio (r) of S-1 to actin, with a peak at r
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Uniquely Stable 40 kDa Subfragment-2 in Carp Myosin
Journal of Agricultural and Food Chemistry, 2005Digestion of carp myofibrils at 30 degrees C in 0.5 M KCl medium with calcium ion generated unique 135 kDa heavy meromyosin (HMM). The HMM was not produced when digested at 10 degrees C. A further digestion of the 135 kD HMM isolated in the absence of calcium ion generated uniquely short subfragment-2 (S-2) with a size of 40 kDa (40 kDa S-2) together ...
Tomoko Tazawa, Takahashi +2 more
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