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Updated: Jun 19, 2026

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Published on: May 1, 2021
Some properties of the protein forming the outer fibers of cilia
F L Renaud1, A J Rowe, I R Gibbons
1Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138.
Abstract:
Cilia were isolated from Tetrahymena pyriformis by an ethanol-calcium procedure. Solutions of outer-fiber protein were obtained either by aqueous extraction of an acetone powder of whole cilia, or by dissolving the isolated outer-fibers in 0.6 M KCl. In aqueous solution, the outer-fiber protein has a sedimentation coefficient of 6.0S and a molecular weight of 104,000 +/- 14,000. In 5 M guanidine hydrochloride solution the molecular weight falls to 55,000 +/- 5,000. After reduction and alkylation in 8 M urea, about 95% of the protein migrates as a single band on electrophoresis in polyacrylamide gel at pH 8.9; the migration velocity is identical with that of reduced and alkylated actin. Freshly prepared outer-fiber protein contains about 7.5 sulfhydryl groups per 55,000 g of protein. The amino acid composition of outer-fiber protein resembles that of actin, with such differences as occur being of the same order as those between actins from different species of animal.
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