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[Structural changes in muscle fiber contractile proteins studied by polarization ultraviolet fluorescence microscopy. VIII. The effect of glutaraldehyde and phalloidine on F-actin conformation].

Iu S Borovikov

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Abstract

Conformational changes in F-actin, induced by glutaraldehyde or phalloidin, were found in glycerinated m. psoas rabbit fibres (ghost and reconstructed fibres). It is shown that the conformational changes of F-actin decreased the thin filament flexibility as well as weakened fibre's contractility. It is assumed that the stabilization in F-actin structure may be an important factor involved in the mechanism of muscle contraction regulation.

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What this paper is about

Conformational changes in F-actin, induced by glutaraldehyde or phalloidin, were found in glycerinated m. psoas rabbit fibres (ghost and reconstructed fibres). It is shown that the conformational changes of F-actin decreased the thin filament flexibility as well as weakened fibre's contractility. It is assumed that the stabilization in F-actin structure may be an important factor involved in the mechanism of muscle contraction regulation.

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Available abstract

Conformational changes in F-actin, induced by glutaraldehyde or phalloidin, were found in glycerinated m. psoas rabbit fibres (ghost and reconstructed fibres). It is shown that the conformational changes of F-actin decreased the thin filament flexibility as well as weakened fibre's contractility. It is assumed that the stabilization in F-actin structure may be an important factor involved in the mechanism of muscle contraction regulation.

Key concepts: Actin, Biophysics, Phalloidin, Glutaraldehyde, Contractility, Chemistry, Protein filament, Fluorescence anisotropy

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[Structural changes in muscle fiber contractile proteins studied by polarization ultraviolet fluorescence microscopy. VIII. The effect of glutaraldehyde and phalloidine on F-actin conformation]. — Research Paper | ScholarLens