Fluorescent actin filaments move on myosin fixed to a glass surface - PubMed (original) (raw)
Fluorescent actin filaments move on myosin fixed to a glass surface
S J Kron et al. Proc Natl Acad Sci U S A. 1986 Sep.
Abstract
Single actin filaments stabilized with fluorescent phalloidin exhibit ATP-dependent movement on myosin filaments fixed to a surface. At pH 7.4 and 24 degrees C, the rates of movement average 3-4 micron/s with skeletal muscle myosin and 1-2 micron/s with Dictyostelium myosin. These rates are very similar to those measured in our previous myosin movement assays. The rates of movement are relatively independent of the type of actin used. The filament velocity shows a broad pH optimum between 7.0 and 9.0, and the concentration of ATP required for half-maximal velocity is 50 microM. Evidence was obtained to suggest that movement of actin over myosin requires at most the number of heads in a single thick filament. This system provides a practical, quantitative myosin-movement assay with purified proteins.
References
- Biochemistry. 1970 Jun 9;9(12):2402-8 - PubMed
- J Cell Biol. 1982 Dec;95(3):711-9 - PubMed
- Biochemistry. 1973 Oct 9;12(21):4206-11 - PubMed
- Proc Natl Acad Sci U S A. 1976 Jan;73(1):165-7 - PubMed
- Proc Natl Acad Sci U S A. 1976 Jul;73(7):2321-5 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources