Distribution and Function of Water and Ions in Resting and Contracted Muscle

Tigyi, J; Káillay, N.; Tigyi-Sebes, A; Trombitás, K

doi:10.1007/978-3-662-39932-3_104

Cited by 2 publications

(3 citation statements)

References 66 publications

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“…As concerns cations, sodium and potassium have been proposed to bind to the myofilament lattice in vitro (McLaughlin and Hinke, 1966;Caille and Hinke, 1973), with direct evidence of potassium binding to the myofilaments shown by Tigyi et al (1981) using ~'2K+ and radioautographic techniques. Seidel (1969) found no evidence that large cations such as cesium and TMA bind to myofilaments.…”

Section: Salt-specific Effects On F~mentioning

confidence: 99%

Ion-specific and general ionic effects on contraction of skinned fast-twitch skeletal muscle from the rabbit.

Andrews

Maughan

Nosek

et al. 1991

The Journal of General Physiology

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We used single fibers from rabbit psoas muscle, chemically skinned with Triton X-100 nonionic detergent, to determine the salts best suited for adjusting ionic strength of bathing solutions for skinned fibers. As criteria we measured maximal calcium-activated force (Fmax), fiber swelling estimated optically, and protein extraction from single fibers determined by polyacrylamide gel electrophoresis with ultrasensitive silver staining. All things considered, the best uniunivalent salt was potassium methanesulfonate, while a number of uni-divalent potassium salts of phosphocreatine, hexamethylenediamine N,N,N',N'-tetraacetic acid, sulfate, and succinate were equally acceptable. Using these salts, we determined that changes in Fma x correlated best with variations of ionic strength (1/2 Z c~ z~, where c~ is the concentration of ion i, and z~ is its valence) rather than ionic equivalents (1/2 ~ c~lz ~ I). Our data indicate that increased ionic strength per se decreases Fma~, probably by destabilizing the cross-bridge structure in addition to increasing electrostatic shielding of actomyosin interactions.

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Section: Salt-specific Effects On F~mentioning

confidence: 99%

Ion-specific and general ionic effects on contraction of skinned fast-twitch skeletal muscle from the rabbit.

Andrews

Maughan

Nosek

et al. 1991

The Journal of General Physiology

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show abstract

“…In all cases K + or its analogue was preferentially located in the A-band, where the heads of myosin are exclusively present, with a fainter electron density at the Z-line. Quantification was obtained with electron probe X-ray microanalysis (see also [73]) and laser microprobe mass-spectroscopic analysis. Autoradiography of single air-dried [19] or frozen fully hydrated muscle fibers [72] using 86 Rb and 134 Cs revealed the same specific localization.…”

Section: Introductionmentioning

confidence: 99%

“…Actin and myosin can be taken as examples of cell-matrix (NUN-) proteins [12, 14, 18, 70, 73, 134]. They possess unfolded regions [14, 75], polarize water [14, 18, 73], adsorb K + [68-73], possess cardinal adsorption sites for ATP and exhibit ATPase activity [12, 14]. It was shown that upon activation of myofibrils weak binding between the S 1 -head of myosin and actin is followed by the release of P i , allowing strong binding, which in turn leads to the power stroke and only then to ADP-release [145].…”

Section: Introductionmentioning

confidence: 99%

Coherent Behavior and the Bound State of Water and K+ Imply Another Model of Bioenergetics: Negative Entropy Instead of High-energy Bonds

Jaeken

Матвеев²

2012

TOBIOCJ

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Observations of coherent cellular behavior cannot be integrated into widely accepted membrane (pump) theory (MT) and its steady state energetics because of the thermal noise of assumed ordinary cell water and freely soluble cytoplasmic K+. However, Ling disproved MT and proposed an alternative based on coherence, showing that rest (R) and action (A) are two different phases of protoplasm with different energy levels. The R-state is a coherent metastable low-entropy state as water and K+ are bound to unfolded proteins. The A-state is the higher-entropy state because water and K+ are free. The R-to-A phase transition is regarded as a mechanism to release energy for biological work, replacing the classical concept of high-energy bonds. Subsequent inactivation during the endergonic A-to-R phase transition needs an input of metabolic energy to restore the low entropy R-state. Matveev’s native aggregation hypothesis allows to integrate the energetic details of globular proteins into this view.

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Distribution and Function of Water and Ions in Resting and Contracted Muscle

Cited by 2 publications

References 66 publications

Ion-specific and general ionic effects on contraction of skinned fast-twitch skeletal muscle from the rabbit.

Ion-specific and general ionic effects on contraction of skinned fast-twitch skeletal muscle from the rabbit.

Coherent Behavior and the Bound State of Water and K+ Imply Another Model of Bioenergetics: Negative Entropy Instead of High-energy Bonds

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