By Kazuhiro Kohama, Yasuharu Sasaki
This ebook explains how gentle muscle contracts in the course of the interplay of myosin with actin, in the context of modern advancements in molecular biology. the main enzyme that phosphorylates myosin to transform it from the inactive shape to the lively shape is myosin gentle chain kinase. The constitution and serve as of this enzyme are defined including the hot findings of its actin-and myosin-binding houses.
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Extra resources for Molecular Mechanisms of Smooth Muscle Contraction (Molecular Biology Intelligence Unit)
The discrepancy is explained in terms of the concentration of actin filaments used in the respective assays. The concentration of actin filaments is much lower in the motility assay (3 nM) than in the ATPase measurement (2 µM) (see ref. 27). The lower concentration of actin filaments requires less MLCK. The Molecular Anatomy of Myosin Light Chain Kinase 21 Fig. 3. 12 (A) Actin cables in internodal cells of Nitellopsis obutusa were exposed by intracellular perfusion. MLCK was then introduced into the cells and allowed to bind to the cables .
17. a) Experiments to narrow the sequence responsible for this actin binding have not yet done. Like parent MLCK, the CNBr fragment is composed of Ca/CaM-sensitive and Ca/CaM-insensitive sites for actin binding and able to assemble actin filaments in a Ca/CaM-sensitive manner. 18 Actin-binding experiments with the NTCB fragment showed that it contains only the Ca/CaM-sensitive site, because: 1. Its binding activity was totally abolished by Ca/CaM;13 and 2. Because it is unable to assemble actin filaments.
J Biol Chem 1984; 259:7740-7746. 11. Yamazaki K, Ito K, Sobue K et al. Purification of caldesmon and myosin light chain (MLC) kinase from arterial smooth muscle: Comparisons with gizzard caldesmon and MLC kinase. J Biochem 1987; 101:1-9. 12. Kohama K, Okagaki T, Hayakawa K et al. A novel regulatory effect of myosin light chain kinase from smooth muscle on the ATP-dependent interaction between actin and myosin. Biochem Biophys Res Commun 1992; 184:1204-1211. 13. Ye L-H, Hayakawa K, Kishi H et al.