FEBS Letters | |
Calcium‐dependent hydrophobic interaction chromatography of calmodulin, troponin C and their proteolytic fragments | |
Thulin, Eva1  Lindahl, Lennart1  Vogel, Hans J.1  | |
[1] Department of Physical Chemistry 2, Chemical Centre, P.O. Box 740, S-220 07 Lund, Sweden | |
关键词: Ca2+/Ca2+-dependence; Calmodulin; Hydrophobic interaction chromatography; Proteolytic-fragment; Troponin C; | |
DOI : 10.1016/0014-5793(83)80554-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The homologous calcium-binding proteins calmodulin and skeletal and cardiac troponin C bind in the presence of 1 mM Ca2+ 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 Ca2+-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 Ca2+-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.
【 授权许可】
Unknown
【 预 览 】
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