The Binding of Ions to the Muscle Proteins. Measurements on the Binding of Potassium and Sodium Ions to Myosin A, Myosin B and Actin<sup>1,2</sup>

Lewis, Marc S.; Saroff, H. A.

doi:10.1021/ja01566a023

Cited by 86 publications

(39 citation statements)

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“…This conclusioil agrees qualitatively with the results of Lewis and Saroff (24). They found that extracted myosin, but not actin, has an affinity for the alkali metal cations, the myosin-sodium complex having a higher association constant than the my osin-potassium con~plex.…”

Section: Discussionsupporting

confidence: 90%

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Optical density changes of single muscle fibers in sodium-free solutions

McLaughlin¹,

Hinke²

1968

Can. J. Physiol. Pharmacol.

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MGLAUGHLIN, S. 6. A., AND HINKE, J. A. M. 1968. optical density changes of single muscle fibers in sodium-free solutions. Can. J. Physiol. Pharrnacol. 46,[247][248][249][250][251][252][253][254][255][256][257][258][259][260] The optical density, O.B., s f single striated muscle fibers frsm the giant barnacle, Balanus izubikl~, was measured at 50-mp intervals between 450 and 850mp. At all wavelengths, the O.D. decreased markedly when the normal Ringer bathing solution was replaced by sodium-free sucrose Ringer solution. For example, at 850 my the O.D. of the fibers, relative to the initial value in normal Ringer solution, decreased from 1 to 0.21 LO.06 in 25 min. The corresponding increase in the transmittance, T, (O.D.--log T ) was from 5 "/, to 55 %. This change in O.D. could be wersed by returning the normal Ringer bathing solution to the bath. Large, reversiblc decreases in O.D. were also observed when potassium and Tris were used as substitutes for sodium. These changes in 0. D. are explained by the theory of light scattering if it is assumed that sodium is bound to rnacromolxules in the myoplasrn. This assumption is supported by experiments with cation-sensitive microelectrodes, which indicate that most of the sodium in the muscle fibers is not free in the myoplasm. When the fibers were bathed in sodium-free, lithiumsubstituted Ringer solution, a small reversible increase in the 0.D. was observed, which may indicate that lithium is complexed more strongly than sodium by macromolecules in the myoplasm. This conclusion is compatible with the known affinities of carboxylate ion exchange resins for the alkali metal cations.

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Section: Discussionsupporting

confidence: 90%

“…The results obtained were compatible with those of Lewis aizd Saroff (24). When the activities of sodium and potassium in a glycerol-extracted barnacle muscle fiber are 0.007 and 0.208 r W respectively, 0.023 mole of sodium is bound per kg of solid fiber material (26).…”

Section: Discussionsupporting

confidence: 80%

Optical density changes of single muscle fibers in sodium-free solutions

McLaughlin¹,

Hinke²

1968

Can. J. Physiol. Pharmacol.

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“…Similar findings were reported by A. Tigyi-Sebes (1962), Ling (1977), Draper (1949Draper ( , 1950, Scott (1932), Szentkuti (1973), Nesterov (1964), Lewis (1957), Mihalyi (1950) etc. In aseries ofstudies we were able to dem onstrate non uniform distribution of the potas- sium atoms inside the musc1e fiber in numerous other cases.…”

Section: Introductionsupporting

confidence: 87%

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

Tigyi¹,

Káillay²,

Tigyi-Sebes

et al. 1981

International Cell Biology 1980–1981

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“…On the other hand, a somewhat stronger bond is likely for a Mn2+ complex if it is of the inner sphere type. Typical literature values for K+ complexing are 9.13 kJ/mol 5 -AGO 5 16.6 kJ/mol (13)(14)(15)(16).…”

Section: Resultsmentioning

confidence: 99%

The structure and equilibria of a manganese(II) complex of fulvic acid studied by ion exchange and nuclear magnetic resonance

Gamble¹,

Langford²,

Tong³

1976

Can. J. Chem.

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The binding of Mn2+ to a well characterized fulvic acid sample is reported based on the competition with K+ in an ion exchange equilibration. The free energy of binding of [Formula: see text] to fulvic acid is only 1–2 kJ/equivalent more favourable than that for K+. This suggests an outer sphere electrostatic structure for the complex. The suggestion is confirmed by observation of minimal change in the presence of fulvic acid of the effect of paramagnetic Mn2+ on the nmr spectra of water. The interpretation of nmr spectra is supported by comparison with nmr measurements of Mn2+ complexes with simple ligands and contrast with nmr measurements on Fe3+ – fulvic acid complexing. The latter is confirmed as inner sphere.

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The Binding of Ions to the Muscle Proteins. Measurements on the Binding of Potassium and Sodium Ions to Myosin A, Myosin B and Actin^1,2

Cited by 86 publications

References 0 publications

Optical density changes of single muscle fibers in sodium-free solutions

Optical density changes of single muscle fibers in sodium-free solutions

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

The structure and equilibria of a manganese(II) complex of fulvic acid studied by ion exchange and nuclear magnetic resonance

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The Binding of Ions to the Muscle Proteins. Measurements on the Binding of Potassium and Sodium Ions to Myosin A, Myosin B and Actin1,2

Cited by 86 publications

References 0 publications

Optical density changes of single muscle fibers in sodium-free solutions

Optical density changes of single muscle fibers in sodium-free solutions

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

The structure and equilibria of a manganese(II) complex of fulvic acid studied by ion exchange and nuclear magnetic resonance

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The Binding of Ions to the Muscle Proteins. Measurements on the Binding of Potassium and Sodium Ions to Myosin A, Myosin B and Actin^1,2