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Purification and partial characterization of a calmodulin‐like protein from cell suspension cultures of Catharanthus roseus
Author(s) -
Radvanyi Laszlo G.,
DiCosmo Frank
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80131-5
Subject(s) - catharanthus roseus , calmodulin , spinach , egta , high performance liquid chromatography , molecular mass , affinity chromatography , biochemistry , chromatography , chemistry , sepharose , calcium , enzyme , organic chemistry
A calmodulin‐like protein was isolated from suspension cultured cells of Catharanthus roseus and purified by a combination of Ca 2+ ‐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 Ca 2+ and had a plant calmodulin‐like UV spectrum and phosphodiesterase‐activation profile.