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Donnan potentials from the A- and I-bands of glycerinated and chemically skinned muscles, relaxed and in rigor - PubMed

Donnan potentials from the A- and I-bands of glycerinated and chemically skinned muscles, relaxed and in rigor

E M Bartels et al. Biophys J. 1985 Jul.

Abstract

Using a combination of microelectrode measurements and high-power microscopy we have demonstrated that different Donnan potentials can be recorded from the A- and I-bands of glycerinated and chemically skinned muscles in rigor, so that the A-band fixed charge concentration exceeds the I-band fixed charge concentration in the rigor condition. In relaxation the two potentials, and therefore the two charge concentrations, are equal in the two bands. X-ray data are presented for relaxed and rigor rat semitendinosus muscle, chemically skinned, and actin and myosin filament charges are calculated under a variety of conditions. Our conclusions are that (a) the fixed (protein) charge is different in the A- and I-bands of striated muscle in the rigor state; (b) the fixed charges are equal in the A- and I-bands of relaxed muscle; (c) the largest charge change between relaxation and rigor is on the thick filament. This occurs whether or not the myosin heads are cross-linked to the thin filaments. (d) Possibly an event on the myosin molecule, the binding of ATP (or certain other ligands) causes a disseminated change that modifies the ion-binding capacity of the myosin rods, or part of them.

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References

1. Biophys J. 1984 Feb;45(2):487-8 - PubMed
1. J Mol Biol. 1973 Jun 5;76(4):519-28 - PubMed
1. J Mol Biol. 1972 Mar 28;65(2):331-45 - PubMed
1. Methods Enzymol. 1982;85 Pt B:20-55 - PubMed
1. Arch Biochem Biophys. 1973 Aug;157(2):573-9 - PubMed

Donnan potentials from the A- and I-bands of glycerinated and chemically skinned muscles, relaxed and in rigor - PubMed