Literature DB >> 3488330

Width and lattice spacing in radially compressed frog skinned muscle fibres at various pH values, magnesium ion concentrations and ionic strengths.

Y Umazume, S Onodera, H Higuchi.   

Abstract

The width (D) and the 1,0 lattice spacing (d1,0) at various ionic compositions of mechanically skinned single fibres (from semitendinosus muscle of Rana catesbeiana) were measured at various concentrations of polyvinyl pyrrolidone (PVP K-30, Mn = 40 000) from 0 to 6% at 20 degrees C. In a standard relaxing solution (4 mM MgATP2-, 1 mM Mg2+, 4 mM EGTA, ionic strength 150 mM and pH 7), d1,0 decreased exponentially as the PVP concentration increased: d1,0 was 41.3 +/- 0.4 (mean +/- S.D.) nm at 0% PVP and 32.9 +/- 0.4 nm at 6% PVP. D was proportional to d1,0 except at very low PVP concentrations, i.e. at 1% PVP, D decreased by 7%, whereas d1,0 decreased by only 3%. At 0% PVP, D and d1,0 decreased when either pH or ionic strength (gamma/2) was lowered. At 6% PVP, D and d1,0 decreased with lowered pH or increased [Mg2+], but was independent of gamma/2. The radial stiffness, or degree of resistance to the changes of D against the compressing force, increased considerably at d1,0 less than or equal to 35 nm in a standard relaxing solution, but not at pH 5.5 or 30 mM [Mg2+]. These effects of pH, [Mg2+] and gamma/2 on D or d1,0 and on the radial stiffness can be explained by the modification of the properties of the elastic element and the hinge between subfragment-1 and -2 and/or the hinge between subfragment-2 and light meromyosin.

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Year:  1986        PMID: 3488330     DOI: 10.1007/BF01753558

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  32 in total

1.  THE BINDING OF DIVALENT CATIONS TO ACTIN.

Authors:  A MARTONOSII; C M MOLINO; J GERGELY
Journal:  J Biol Chem       Date:  1964-04       Impact factor: 5.157

2.  Electro-optical property of extremely stretched skinned muscle fibers.

Authors:  Y Umazume; S Fujime
Journal:  Biophys J       Date:  1975-02       Impact factor: 4.033

3.  New elastic protein from muscle.

Authors:  K Maruyama; R Natori; Y Nonomura
Journal:  Nature       Date:  1976-07-01       Impact factor: 49.962

4.  Force-balances and stability in hexagonally-packed polyelectrolyte systems.

Authors:  G F Elliott
Journal:  J Theor Biol       Date:  1968-10       Impact factor: 2.691

5.  Localization of the parallel elastic components in frog skinned muscle fibers studied by the dissociation of the A- and I-bands.

Authors:  H Higuchi; Y Umazume
Journal:  Biophys J       Date:  1985-07       Impact factor: 4.033

6.  Axial elastic modulus as a function of relative fiber width in relaxed skinned skeletal muscle fibers.

Authors:  M R Berman; D W Maughan
Journal:  Pflugers Arch       Date:  1982-03       Impact factor: 3.657

7.  X-ray diffraction observations of chemically skinned frog skeletal muscle processed by an improved method.

Authors:  A Magid; M K Reedy
Journal:  Biophys J       Date:  1980-04       Impact factor: 4.033

8.  Lateral forces in the filament lattice of vertebrate striated muscle in the rigor state.

Authors:  B M Millman; K Wakabayashi; T J Racey
Journal:  Biophys J       Date:  1983-03       Impact factor: 4.033

9.  Titin: major myofibrillar components of striated muscle.

Authors:  K Wang; J McClure; A Tu
Journal:  Proc Natl Acad Sci U S A       Date:  1979-08       Impact factor: 11.205

10.  The myofilament lattice: studies on isolated fibers. II. The effects of osmotic strength, ionic concentration, and pH upon the unit-cell volume.

Authors:  E W April; P W Brandt; G F Elliott
Journal:  J Cell Biol       Date:  1972-04       Impact factor: 10.539

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  20 in total

1.  Parvalbumin concentration and diffusion coefficient in frog myoplasm.

Authors:  D W Maughan; R E Godt
Journal:  J Muscle Res Cell Motil       Date:  1999-02       Impact factor: 2.698

2.  Diffraction ellipsometry studies of osmotically compressed muscle fibers.

Authors:  W L Kerr; R J Baskin; Y Yeh
Journal:  Pflugers Arch       Date:  1990-08       Impact factor: 3.657

3.  Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy.

Authors:  Daisuke Miyashiro; Jun'ichi Wakayama; Nao Akiyama; Yuki Kunioka; Takenori Yamada
Journal:  J Physiol Sci       Date:  2013-05-21       Impact factor: 2.781

4.  The direct molecular effects of fatigue and myosin regulatory light chain phosphorylation on the actomyosin contractile apparatus.

Authors:  Michael J Greenberg; Tanya R Mealy; Michelle Jones; Danuta Szczesna-Cordary; Jeffrey R Moore
Journal:  Am J Physiol Regul Integr Comp Physiol       Date:  2010-01-20       Impact factor: 3.619

5.  Cross-bridge movement in rat slow skeletal muscle as a function of calcium concentration.

Authors:  H Honda; Y Koiwa; N Yagi; I Matsubara
Journal:  Pflugers Arch       Date:  1996-09       Impact factor: 3.657

6.  Weakly attached cross-bridges in relaxed frog muscle fibers.

Authors:  D W Jung; T Blangé; H de Graaf; B W Treijtel
Journal:  Biophys J       Date:  1989-04       Impact factor: 4.033

7.  Low cell pH depresses peak power in rat skeletal muscle fibres at both 30 degrees C and 15 degrees C: implications for muscle fatigue.

Authors:  S T Knuth; H Dave; J R Peters; R H Fitts
Journal:  J Physiol       Date:  2006-06-29       Impact factor: 5.182

8.  Deterioration induced by physiological concentration of calcium ions in skinned muscle fibres.

Authors:  N Kasuga; Y Umazume
Journal:  J Muscle Res Cell Motil       Date:  1990-02       Impact factor: 2.698

9.  Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibres from rabbit.

Authors:  P B Chase; D A Martyn; M J Kushmerick; A M Gordon
Journal:  J Physiol       Date:  1993-01       Impact factor: 5.182

10.  Myosin heads contact with thin filaments in compressed relaxed skinned fibres of frog skeletal muscle.

Authors:  Y Umazume; H Higuchi; S Takemori
Journal:  J Muscle Res Cell Motil       Date:  1991-10       Impact factor: 2.698

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