Literature DB >> 3407373

Purification of rabbit skeletal muscle troponin C.

E Thulin1, H J Vogel.   

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.

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Year:  1988        PMID: 3407373     DOI: 10.3891/acta.chem.scand.42b-0211

Source DB:  PubMed          Journal:  Acta Chem Scand B        ISSN: 0302-4369


  2 in total

1.  Utilization of troponin C as a model calcium-binding protein for mapping of the calmodulin-binding sites of caldesmon.

Authors:  A A Polyakov; N B Gusev
Journal:  Biochem J       Date:  1997-02-01       Impact factor: 3.857

Review 2.  Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides.

Authors:  Aaron P Yamniuk; Hans J Vogel
Journal:  Mol Biotechnol       Date:  2004-05       Impact factor: 2.695

  2 in total

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