IDENTIFICATION AND CHARACTERIZATION OF TETRAHYMENA MYOSIN

Myosin was partially purified from ciliated protozoan Tetrahymena pyri formis. Tetrahymena myosin has a fibrous tail with two globular heads at one end and contains 220-kDa heavy chains. The tail length of the m olecule (200 nm) is longer than that of myosins from other animals (ap proximately 160 nm). A sample after HPLC column chromatography contain ing 220-kDa peptide showed a myosin-specific K+-/NH4+-EDTA-ATPase acti vity. Polyclonal anti-crayfish myosin heavy chain antibody reacted wit h Tetrahymena 220-kDa myosin heavy chain, and monoclonal anti-pan myos in antibody reacted with Tetrahymena 180-kDa peptide. The isolated 180 -kDa peptide was identified as a clathrin heavy chain. Copyright (C) 1 996 Elsevier Science Inc.