Abstract
Pellicles of the ciliate T. pyriformis strain GL (phenoset A) were isolated by a new procedure. Oral apparati were purified by a modification of a previous method. Both preparations were characterized by EM. Proteins of the isolates were separated by analytical SDS [sodium dodecyl sulfate] polyacrylamide gel electrophoresis. The isolated pellicles which included oral apparati, contained only 6 major proteins (gel bands), designated A through F. Bands A, B and C were found in the pellicle fraction, but not in the oral apparatus fraction. These proteins were probably present in the somatic cortex of Tetrahymena. Bands D and E were greatly enriched in the oral apparatus fraction; these proteins were probably present primarily in the oral apparatus. Band F identified as tubulin, was present in both preparations. Molecular weight determinations and some selective solubilization experiments were presented.