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Rapid purification and identification of calcyphosine, a Ca(2+)-binding protein phosphorylated by protein kinase A.

par Lecocq, R;Lamy, Françoise ;Erneux, Christophe ;Dumont, Jacques Emile
Référence Biochemical journal, 306, 1, page (147-151)
Publication Publié, 1995-02

Article révisé par les pairs

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Résumé :

A method is presented for the rapid purification of dog thyroid calcyphosine, a protein previously identified as a major substrate for cyclic AMP-dependent protein kinase in dog thyroid slices stimulated by thyrotropin [Lecocq, Lamy and Dumont (1979) Eur. J. Biochem. 102, 147-152]. The protein was previously identified as a spot on two-dimensional gels and is now purified in its native form by a procedure involving three chromatographic steps. Homogeneous calcyphosine identified by SDS/PAGE, immunoblotting and peptide sequencing can be obtained within 7 h. As for calmodulin, Ca(2+)-dependent conformational changes can be shown by Ca(2+)-dependent hydrophobic interaction chromatography using phenyl-Sepharose. Unlike calmodulin, calcyphosine is a substrate for protein kinase A.