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- W983337617 abstract "This chapter describes a purification procedure for MHC kinase A that results in the isolation of an unphosphorylated form of the enzyme and describes a more rapid procedure for the isolation of a highly phosphorylated form of MHC kinase A. Phosphorylation of the myosin II heavy chain occurs in many vertebrate nonmuscle cell types and in the lower eukaryotes Acanthamoeba and Dictyostelium as well as in vertebrate smooth muscle and invertebrate catch muscle. The kinases responsible for phosphorylation of the vertebrate myosin II heavy chains have been identified variously as casein kinase II in brain, a Ca2+calmodulin-dependent kinase in brain and intestinal brush border cells, and protein kinase C in platelets. A myosin II heavy chain kinase (MHC kinase A) is purified from Dictyostelium that phosphorylates two residues (Thr-1833 and Thr-2029) within the carboxyl-terminal one-quarter of the Dictyostelium myosin II tail. Phosphorylation of Dictyostelium myosin II at these sites results in the destabilization of myosin II bipolar filaments and inhibition of the myosin II actin-activated Mg 2+ -ATPase activity." @default.
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- W983337617 date "1991-01-01" @default.
- W983337617 modified "2023-10-14" @default.
- W983337617 title "[3] Purification and characterization of myosin II heavy chain kinase A from Dictyostelium" @default.
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- W983337617 doi "https://doi.org/10.1016/0076-6879(91)96005-c" @default.
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