Purification and characterization of Tetrahymena profilin.
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.
Edamatsu
M
M
Institute of Biological Sciences, University of Tsukuba, Ibaraki, Japan.
Hirono
M
M
Watanabe
Y
Y
D000199:Actins / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity; D003285:Contractile Proteins; D008840:Microfilament Proteins / Q000032:analysis*; D051304:Profilins; D011817:Rabbits; D013768:Tetrahymena / Q000032:analysis*; D014783:Viscosity
D000199:Actins; D003285:Contractile Proteins; D008840:Microfilament Proteins; D051304:Profilins