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ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle.
Open accessAbstract
The rate constant for dissociation of ADP from actomyosin subfragment 1 (S1) has been measured in this laboratory and elsewhere for a variety of vertebrate muscle types. We have made the following observations: (i) In solution, the dissociation of ADP from actomyosin-S1 limits the rate of dissociation of actomyosin-S1-ADP by ATP and, presumably, also limits the rate of crossbridge detachment in contracting muscle. (ii) For muscle types in which the rate of ADP dissociation from actomyosin-S1 is slow enough to measure using stopped-flow methods, the rate constants are nearly the same as the theoretical value for the minimum allowable rate constant for dissociation of an attached crossbridge. Therefore, ADP dissociation is sufficiently slow to be the molecular step that limits the maximum shortening velocity of these muscles. (iii) Variation with muscle type of the rate constant for ADP dissociation may be a general phylogenetic mechanism for regulating shortening velocity.
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Citations
Cites
Dissociation of the actin.subfragment 1 complex by adenyl-5'-yl imidodiphosphate, ADP, and PPi.
Greene, L. E., & Eisenberg, E. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86209-9 · Cited by 151
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Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022
Bottinelli, R., Canepari, M., Pellegrino, M. A., & Reggiani, C. (1996) · The Journal of Physiology · doi:10.1113/jphysiol.1996.sp021617 · Cited by 565
The Molecular Mechanism of Muscle Contraction
Geeves, M. A., & Holmes, K. C. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(04)71005-0 · Cited by 398
Godt, R. E., & Nosek, T. M. (1989) · The Journal of Physiology · doi:10.1113/jphysiol.1989.sp017609 · Cited by 323
Kinetic Mechanism of Non-muscle Myosin IIB
Wang, F., Kovács, M., Hu, A., Limouze, J., Harvey, E. V., & Sellers, J. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302510200 · Cited by 253
Metadata
- Authors
- Siemankowski, R. F., Wiseman, M. O., & White, H. D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1985-02
- Volume
- 82
- Issue
- 3
- Pages
- 658-662
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2030547704
- Cited by
- 410
- References
- 1
- FWCI
- 4.09
- Type
- journal article
- Language
- en
- Open access
- green
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- Siemankowski, R. F., Wiseman, M. O., & White, H. D. (1985). ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.82.3.658
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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