Presence of calmodulin in Tetrahymena.
- 1 December 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (12) , 6471-6475
- https://doi.org/10.1073/pnas.76.12.6471
Abstract
Ca-dependent affinity chromatography on phenothiazine-Sepharose 4B was used to isolate a pure protein from the ciliate T. pyriformis. This protein was identified as calmodulin by demonstrating 3 of the Ca-dependent activities attributed to calmodulins. Tetrahymena calmodulin also has physicochemical properties similar to those of the previously characterized mammalian, coelenterate and plant proteins, except for a lower MW (15,000) and slightly different CNBr fragments compared to bovine brain calmodulin. Calmodulin is a constituent of demembranated Tetrahymena cilia from which it can be extracted with the crude dynein fraction. Sucrose density gradient fractionation indicated its presence in fractions containing the 14S dynein ATPase. The essential properties of calmodulin probably were highly conserved during much of eukaryotic evolution, and calmodulin may play a role in the control of ciliary motility in Tetrahymena.This publication has 37 references indexed in Scilit:
- Calcium-dependent affinity chromatography of calmodulin on an immobilized phenothiazineBiochemical and Biophysical Research Communications, 1979
- Purification of plant calmodulin by fluphenazine-Sepharose affinity chromatographyBiochemical and Biophysical Research Communications, 1979
- Isolation and characterization of calcium(2+) ion-dependent modulator protein from the marine invertebrate Renilla reniformisBiochemistry, 1979
- Calcium-dependent regulator of NAD kinase in higher plantsBiochemical and Biophysical Research Communications, 1978
- High levels of a calcium-dependent modulator protein in spermatozoa and its similarity to brain modulator proteinBiochemical and Biophysical Research Communications, 1978
- Partial purification of the Ca2+-Mg2+ ATPase activator from human erythrocytes: Its similarity to the activator of 3′:5′ — cyclic nucleotide phosphodiesteraseBiochemical and Biophysical Research Communications, 1977
- Phosphodiesterase protein activator mimics red blood cell cytoplasmic activator of (Ca2+-Mg2+)ATPaseBiochemical and Biophysical Research Communications, 1977
- The distribution of the Ca++-dependent protein activator of cyclic nucleotide phosphodiesterase in invertebratesBiochemical and Biophysical Research Communications, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Cyclic 3′,5′-nucleotide phosphodiesteraseBiochemical and Biophysical Research Communications, 1970