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

@article{Prchniewicz1990InhibitionOS,
  title={Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility.},
  author={Ewa Pr{\'o}chniewicz and Toshio Yanagida},
  journal={Journal of molecular biology},
  year={1990},
  volume={216 3},
  pages={761-72}
}
The effects of crosslinking of monomeric and polymeric actin with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC), disuccinimidyl suberate (DSS) and glutaraldehyde on the interaction with heavy meromyosin (HMM) in solution and on the sliding movement on glass-attached HMM were examined. The Vmax values of actin-activated HMM ATPase decreased in the following order: intact actin = EDC F-actin greater than DSS actin greater than glutaraldehyde F-actin = glutaraldehyde G-actin greater than EDC… CONTINUE READING

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