Identification and characterization of Tetrahymena myosin |
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| Authors: | Nobuyuki Kanzawa Osamu Numata Yoshio Watanabe Koscak Maruyama |
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| Institution: | aDepartment of Biology, Faculty of Science, Chiba University, Chiba 263, Japan;bInstitute of Biological Sciences, University of Tsukuba, Ibaraki 305, Japan |
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| Abstract: | Myosin was partially purified from ciliated protozoan Tetrahymena pyriformis. Tetrahymena myosin has a fibrous tail with two globular heads at one end and contains 220-kDa heavy chains. The tail length of the molecule (200 nm) is longer than that of myosins from other animals (approximately 160 nm). A sample after HPLC column chromatography containing 220-kDa peptide showed a myosin-specific K+-/NH4+-EDTA-ATPase activity. Polyclonal anti-crayfish myosin heavy chain antibody reacted with Tetrahymena 220-kDa myosin heavy chain, and monoclonal anti-pan myosin antibody reacted with Tetrahymena 180-kDa peptide. The isolated 180-kDa peptide was identified as a clathrin heavy chain. |
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| Keywords: | Myosin clathrin myosin-ATPase K+-/NH4+-EDTA-ATPase Tetrahymena myosin protozoa myosin anti-crayfish myosin heavy chain antibody anti-pan myosin antibody |
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