Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility.

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Summary

Examination of the effects of crosslinking of monomeric and polymeric actin with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, disuccinimidyl suberate and glutaraldehyde on the interaction with heavy meromyosin in solution and on the sliding movement concluded that movement is generated by interaction of myosin with segments of F-actin containing a number of intact monomers.

Type
article
Published
1990-12-05
Cited by
91
References
34

Keywords

Glutaraldehyde, Actin, Heavy meromyosin, Myosin, Biophysics

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