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Purification and characterization of Tetrahymena profilin
M Edamatsu1, M Hirono, Y Watanabe
1Institute of Biological Sciences, University of Tsukuba, Ibaraki, Japan.
Biochemical and Biophysical Research Communications
|July 31, 1990
Abstract:
We subjected Tetrahymena cell extract to a poly(L-proline) affinity column for isolating profilin and obtained a protein of 12.8 kDa. Purified 12.8 kDa protein dose-dependently inhibited the polymerization of Tetrahymena actin more strongly than that of rabbit skeletal muscle actin. Because the 12.8 kDa protein fulfills properties common to profilins, the protein is considered to be Tetrahymena profilin. The present paper is the first report of the isolation of an actin-binding protein from Tetrahymena.