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- W1006901431 abstract "This chapter describes procedures for the purification of Myosin light chain kinase (MLC kinase) from a number of sources; from gizzard smooth muscle, emphasizing two different preparations favored by two laboratories. These two preparations are presented in detail and two other preparations from different smooth muscles are outlined. Two different methods for preparing Ca2+/calmodulin-independent smooth muscle MLC kinase are described. A number of laboratories to study the properties of the enzyme as well as its role in smooth muscle and nonmuscle cells have utilized this proteolytic fragment. MLC kinase catalyses the transfer of the γ-phosphate of ATP to the regulatory light chain (also known as the P-light chain) of the major contractile protein myosin. Myosin is composed of a pair of heavy chains (Mr 200,000) and two pairs of light chains. In smooth muscles, MLC kinase catalyzes the phosphorylation of serine-19, and under certain circumstances, of threonine-18. In skeletal muscle, only the analogous serine residue appears to be phosphorylated." @default.
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- W1006901431 date "1991-01-01" @default.
- W1006901431 modified "2023-10-17" @default.
- W1006901431 title "[4] Purification and properties of myosin light chain kinases" @default.
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- W1006901431 doi "https://doi.org/10.1016/0076-6879(91)96006-d" @default.
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