Purification of Rabbit Skeletal Muscle Troponin C.
- 1 January 1988
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 42b (4) , 211-215
- https://doi.org/10.3891/acta.chem.scand.42b-0211
Abstract
Troponin C binds to phenyl-Sepharose in the presence of Ca2+ and can be eluted with EDTA. This property was used as an essential step in the purification of this protein from rabbit skeletal muscle. Troponin C was extracted with 6M urea from extensively washed ground muscle. The protein was bound to and eluted from DEAE-Sephadex, fractionated by size on Sephadex G75, and in a final step purified from UV-absorbing non-protein impurities on phenyl-Sepharose. The total yield of electrophoretically pure protein was 60 mg per 100 g of muscle, which is considerably higher than that previously obtained.This publication has 15 references indexed in Scilit:
- A structural role for the Ca2+-Mg2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils.Published by Elsevier ,2021
- Ca2+-dependent hydrophobic-interaction chromatography. Isolation of a novel Ca2+-binding protein and protein kinase C from bovine brainBiochemical Journal, 1984
- Metal-ion-dependent hydrophobic-interaction chromatography of α-lactalbuminsAnalytical Biochemistry, 1984
- Rapid purification of calsequestrin from cardiac and skeletal muscle sarcoplasmic reticulum vesicles by Ca2+-dependent elution from phenyl-sepharose.Journal of Biological Chemistry, 1983
- Cloning and characterization of cDNA sequences corresponding to myosin light chains 1, 2, and 3, troponin-C, troponin-T, alpha-tropomyosin, and alpha-actin.Journal of Biological Chemistry, 1982
- Ca2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatographyBiochemical and Biophysical Research Communications, 1982
- Calmodulin-free skeletal-muscle troponin C prepared in the absence of ureaBiochemical Journal, 1981
- Proteolytic fragments of troponin C. Localization of high and low affinity Ca2+ binding sites and interactions with troponin I and troponin TJournal of Biological Chemistry, 1978
- Ca2+, Mg2+dependent conformations of troponin C as determined by 1H and 19F nuclear magnetic resonanceBiochemistry, 1977
- Conformational transition accompanying the binding of calcium(2+) ion to the protein activator of 3',5'-cyclic adenosine monophosphate phosphodiesteraseBiochemistry, 1977