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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 15890-15894 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 5864-5871 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 68 (1999), S. 687-728 
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Notes: Abstract X-ray crystallography shows the myosin cross-bridge to exist in two conformations, the beginning and end of the "power stroke." A long lever-arm undergoes a 60o to 70o rotation between the two states. This rotation is coupled with changes in the active site (OPEN to CLOSED) and phosphate release. Actin binding mediates the transition from CLOSED to OPEN. Kinetics shows that the binding of myosin to actin is a two-step process which affects ATP and ADP affinity. The structural basis of these effects is not explained by the presently known conformers of myosin. Therefore, other states of the myosin cross-bridge must exist. Moreover, cryoelectronmicroscopy has revealed other angles of the cross-bridge lever arm induced by ADP binding. These structural states are presently being characterized by site-directed mutagenesis coupled with kinetic analysis.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 16 (1995), S. 412-419 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Effects of increased hydrostatic pressure (range 0.1–10 MPa) on isometric twitch and tetanic contractions of single intact muscle fibres, isolated from frog tibialis anterior muscle, were examined at 4–12° C. The tension changes produced on exposure to steady high pressures are compared with those produced on exposure to low concentrations of caffeine (0.5 mm, subthreshold for contracture) and when pressure is rapidly released during a contraction. The peak twitch tension was potentiated by pressure accompanied by increased rate of tension rise and increased duration; the pressure sensitivity of twitch tension was ≈8% mPa-1. The correlation between the rate of tension rise and peak tension in caffeine-induced twitch tension potentiation was quantitatively similar to that in pressure-induced twitch potentiation. Experiments involving the rapid release of pressure (≈2 ms) during twitch contractions demonstrate that high pressure need only be maintained for a brief period during the early part of tension development to elicit full twitch potentiation. The tetanic tension was depressed by pressure (≈1% MPa-1). Results demonstrate that the major effect of increased hydrostatic pressure on intact muscle fibres, which results in tension potentiation, is complete very early during contraction and is similar to that of caffeine.
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  • 5
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 2,3-butanedione 2-monoxime (BDM) inhibits muscle contraction and actomyosin ATPase both in fibres and in solution. It is potentially useful as a tool for exploring weak interactions between actin and myosin. We have examined the effect of BDM on several key steps of the myosin subfragment-1 and actomyosin subfragment-1 ATPase in solution. These studies show that BDM shifts the equilibrium between two actomyosin states towards a more weakly bound form when the acto.myosin complex has ADP alone or ADP and phosphate bound. We also confirm the findings of Herrmann and colleagues (1993, Biochemistry, 31, 12227–32) that the main effect of BDM on the myosin subfragment-1 ATPase is to slow the release of phosphate following ATP hydrolysis. Skinned fibre studies show that the effects of BDM and phosphate on the steady isometric tension of the fibres are additive. This is consistent with the interpretation that BDM is reducing fibre tension either by increasing phosphate binding or by a direct effect on the crossbridge. Tension transients induced by rapid pressure release were examined in single muscle fibres; they showed that BDM reduces the rate of tension generation following pressure release. This result suggest that BDM directly affects the force generating event in the crossbridge. Since we submitted this paper, Y. Zhao and M. Kawai have published evidence that BDM reduces the equilibrium constant of the power stroke step in rabbit psoas muscle fibres (Am. J. Physiol. 266, C437-47 (1994)). This is consistent with the main findings in our work.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 17 (1996), S. 631-636 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Effects of increased hydrostatic pressure (range 0.1–10 MPa) on isometric twitch and tetanic contractions of single, intact, frog muscle fibres were examined at 4, 11 and 21°C and at different stages of fatigue. Twitch tension was potentiated by pressure at all temperatures, but the extent of potentiation was more pronounced at higher temperatures (34% MPa-1 at 21°C, compared to 8% MPa-1 at 4°C). Tetanic tension was depressed by pressure at 4°C (∼0.7% MPa-1) but was potentiated by pressure at 21°C (∼0.4% MPa-1). The effect of hydrostatic pressure on the tetanic tension was dependent on the fatigue status of the muscle fibre: during the early stages of fatigue (when tetanic tension was depressed by 〈20%), high pressure produced a tension depression (as in an unfatigued muscle fibre), whilst during the later stages of fatigue high pressure induced a significant potentiation of tetanic tension. Our results support the suggestion that excitation-contraction coupling and contractile activation are impaired during late fatigue. Pressure-effects were basically similar to caffeine-effects under a variety of conditions, suggesting that an enhancement of Ca2+ release may be contributory to potentiation of twitch tension and, in severely, fatigued muscle, potentiation of tetanic tension. In the rested state and during early fatigue the main effect of pressure is an inhibition of the crossbridge cycle.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 10 (1989), S. 113-123 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The effect of changes in hydrostatic pressure (up to 10 MPa) on the maximally calcium-activated tension in glycerinated rabbit psoas fibres has been examined. The steady active tension was depressed by 0.8% per MPa pressure rise. This pressure sensitivity was enhanced by the presence of millimolar phosphate and depressed by millimolar ADP. These results support the conclusions that increased pressure is perturbing a crossbridge event. The results are discussed in terms of a three state crossbridge model and are shown to be compatible with a pressure effect on the transition from an attached crossbridge state to a tension bearing state. This is compatible with the effects of pressure on the isolated proteins in solution.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 5 (1984), S. 351-361 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Recent experiments on the kinetics of the interaction between myosin subfragment 1 (S1) and F-actin in solution are summarized. It is concluded that, at every step of the ATPase cycle, the association between the two proteins takes place in two stages. The equilibrium constant of the second step and thus the affinity of S1 for actin changes from step to step during the enzymatic reaction. It is proposed that the transient kinetic evidence can be interpreted in terms of two different classes of contraction models. The first one, which is widely used at present, identifies particular steps in the enzymatic reaction as directly responsible for the conformational change which represents the power stroke of muscle contraction (direct coupling model). In the second class of model, to which we wish to draw attention, changes in affinity modulated by the enzymatic reaction result in changes in the relative amounts of time spent by parts of the myosin molecule in two different environments. These environments determine whether the molecule exists in the ‘long’ or ‘short’ state, and it is the transition between these two which constitutes the power stroke (indirect coupling model).
    Type of Medium: Electronic Resource
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  • 9
    Publication Date: 1993-09-15
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 10
    Publication Date: 2008-04-07
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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