FEBS Letters · 1983 · 93 citations · 34 references
Life SciencesBiochemistryMolecular BiologyChromatographic AnalysisProtein BiochemistryProteomicsCalcium-binding ProteinsChromatographic PurificationHydrophobic Interaction ChromatographyProtein PurificationProtein SeparationProtein StructureCalcium AffinityCalcium BiochemistryCalcium-binding Site StructureCalcium-dependent Protein-protein InteractionsCalcium-mediated SignalingCardiac TroponinsHydrophobic InteractionsTroponin C
The homologous calcium‐binding proteins calmodulin and skeletal and cardiac troponin C bind in the presence of 1 mM Ca 2+ to phenyl‐Sepharose and can be eluted in buffers containing chelators. Results obtained with a series of proteolytic fragments, which were prepared by limited tryptic or thrombic degradation, showed that this Ca 2+ ‐dependent hydrophobic interaction chromatography provides a convenient method for the large scale purification of some of these peptides. Moreover, it was found that in troponin C only one Ca 2+ ‐induced hydrophobic site is located in the amino‐terminal half of the protein, but that calmodulin contained such sites in both the amino‐ and carboxy‐terminal halves of the molecule. The probable location of the latter site is discussed.
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