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  • 1995-1999  (1)
  • 1980-1984  (7)
  • 1965-1969  (3)
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 378 (1995), S. 209-212 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Previous studies7 9, under conditions in which several molecules are interacting with the actin filament, indicated that both SI and single-headed myosin are capable of generating movement and force. To demonstrate that such events occur between a single myosin head and an actin monomer, we have ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 222 (1969), S. 1184-1185 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fibres of glycerol-extracted flight muscle from the water-bug Lethocerus cordofanus, provided with MgATP and Ca2+ and subjected to a forced longitudinal oscillation, will work in a way analogous to their performance during flight; in optimal conditions a large part of the myosin is activated in ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 207 (1965), S. 1276-1280 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] MYOGENIC fibrillar insect flight muscle is known to perform considerable work by means of small-amplitude oscillations both in life1 and when glycerinated2. The structure of the muscle is exceptionally well ordered3"4. Electron microscope studies indicate that the ends of the myosin filaments are ...
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 205 (1965), S. 600-601 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig, 1. Impedance of akin in contact with 0.9 per cent sodium chloride as a function of frequency of applied alternating current I have investigated how the impedance to low-frequency a.c. recorded from skin is influenced by the way in which contact is made with the skin surface. A circular metal ...
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 2 (1981), S. 345-345 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 3 (1982), S. 375-375 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 5 (1984), S. 687-696 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Insect flight muscle fibres were relaxed by the combined action of MgAMPPNP and ethylene glycol, as measured by the stiffness of the fibres. Relaxation occurred over a small range of glycol concentration. Addition of Ca2+ raised the glycol required for relaxation. The speed at which the stiffness measurement was made did not influence the glycol concentration at which relaxation occurred. Glycol in excess of that needed to relax the muscle caused a slight rise in high-frequency stiffness. Removal of the glycol restored the rigor stiffness. Under glycol-relaxed conditions, much of the AMPPNP bound in muscle fibres was retained during cold-chase (elution of [3H] AMPPNP by nonradioactive AMPPNP); the intensity ratio of the inner equatorial X-ray diffraction peaks rose upon glycol relaxation to a value slightly below that characteristic of natural relaxation. The results are interpreted in terms of cooperative attachment of the crossbridges to actin.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 4 (1983), S. 543-556 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary When a small bundle of glycerol-extracted fibres from either frog, tortoise or rabbit skeletal muscle was first exposed to high MgATP (5mm) in the absence of Ca2+ (〈1nm) and at low ionic strength (〈0.11) at 20° C, it produced a single sharp transient contraction followed by a lower maintained isometric tension. The maintained tension was investigated further in rabbit psoas fibres. Ca2+-free tension was dependent on the ionic strength in the range 0.04–0.10, on the temperature in the range 6–20° C and the free Mg2+ in the range 0–6mm. It was promoted by low ionic strength, low Mg2+ and high temperature, and was unaffected by varying the MgATP2− in the range 0.4–4mm and by adding ATP regenerating components. A separate regime of tension generation was detected at MgATP2− concentrations of less than 0.1mm, in which MgATP2− concentration was critical. The results are interpreted on the assumption that binding of Mg2+ to some component of the regulatory system is necessary to maintain its inhibitory effect in the absence of Ca2+. Ionic strength and temperature, on the other hand, may affect actomyosin directly.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 1 (1980), S. 1-2 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 5 (1984), S. 81-96 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Substitution of ethylene glycol for part of the solvent water changes the mechanical properties, structure and nucleotide binding of glycerol-extracted flight muscle fibres from the waterbugLethocerus. On addition of ethylene glycol the rigor tension falls, rapidly and reversibly. With increasing glycol concentration the effect saturates at a non-zero tension. The isotonic stiffness is unchanged on adding ethylene glycol. Adding MgAMPPNP (adenylylimidodiphosphate) to a muscle fibre in 50% ethylene glycol causes a further rapid tension fall; above 100 µm AMPPNP the tension reaches zero. The isotonic stiffness of restretched muscle is then close to that of a relaxed fibre. Removal of MgAMPPNP from the bathing medium has no immediate mechanical effect. After several hours the isotonic stiffness rises to some extent; on removal of the glycol both tension and stiffness rise to rigor values within one minute.3H-Labelled AMPPNP binds to muscle fibres in 50% ethylene glycol in a similar amount to the number of myosin heads present. The binding is tighter than that in aqueous solution and the nucleotide is only released very slowly. Upon removal of the ethylene glycol nucleotide is rapidly released. X-ray diffraction of muscle in 50% ethylene glycol reveals a highly ordered structure, in which both the 14 nm and the 38 nm layer lines are sharply sampled and are of intermediate values between rigor and relaxation. The two inner equatorial peaks are also of intermediate values. On adding MgAMPPNP the pattern resembles that of relaxed muscle. Upon removal of the nucleotide the pattern does not revert towards rigor but on removal of glycol it does. These results are interpreted in terms of changes within the myosin heads and their array within the filament lattice.
    Type of Medium: Electronic Resource
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