Abstract:
:When skinned skeletal muscle fibres with rest sarcomere length (L = 2.5 microns) are compressed by the addition of various concentrations ([PVP]) of polyvinylpyrrolidine, the relation between the 1,0 spacing (d) of thick filament lattice and [PVP] has been known to break at d of around 35 nm, resulting in a steeper slope of the relationship at d greater than 35 nm. To clarify the cause of this, X-ray diffraction and crosslinking experiments were carried out. The d versus [PVP] relationship of stretched fibres (L = 3.5 microns) breaks at a d of around 29 nm. The difference between these characteristic d values, 35-29 = 6 nm, is close to the diameter of thin filaments (8 nm). The crosslinking efficiency of formaldehyde between myosin heads and thin filament surface, measured by radial stiffness increase, was found to begin to markedly increase when the relaxed fibre with rest L was compressed to a d of nearly 35 nm. In addition to these results, the d versus [PVP] relationship obtained in rigor and in high [Mg2+] (30 mM) relaxing solutions, and the crosslinking efficiency seen in high [Mg2+] solutions supported our previous hypothesis that in normal relaxing solution (containing 1 mM Mg2+) the probability of myosin heads coming into contact with the thin filament surface abruptly increases at d near 35 nm in fibres with rest L.
journal_name
J Muscle Res Cell Motiljournal_title
Journal of muscle research and cell motilityauthors
Umazume Y,Higuchi H,Takemori Sdoi
10.1007/BF01738331subject
Has Abstractpub_date
1991-10-01 00:00:00pages
466-71issue
5eissn
0142-4319issn
1573-2657journal_volume
12pub_type
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
pub_type: 传,历史文章,杂志文章
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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