Calcium‐dependent hydrophobic interaction chromatography of calmodulin, troponin C and their proteolytic fragments

FEBS Letters

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