Purification and partial characterization of a calmodulin-like protein from cell suspension cultures of Catharanthus roseus

AbstractA calmodulin-like protein was isolated from suspension cultured cells of Catharanthus roseus and purified by a combination of Ca2+-facilitated phenyl-Sepharose affinity chromatography and reverse-phase HPLC. The HPLC-purified protein was analysed using SDS-PAGE and found to be a homogeneous 19.5 kDa band in gels containing 1 mM EGTA unlike a higher plant calmodulin from spinach which migrated as a 17.38 kDa band. Despite this apparent difference in molecular mass, the purified protein showed a similar increase in electrophoretic mobility (4010 Da) to spinach calmodulin (4200 Da) in gels containing 1 mM Ca2+ and had a plant calmodulin-like UV spectrum and phosphodiesterase-activation profile