Identification of a 55-kDa high-affinity calmodulin-binding protein from Electrophorus electricus.
A high-affinity calcium-dependent calmodulin-binding protein (CaMBP) has been isolated from Electrophorus electricus main electric organ. This 55-kDa CaMBP has been purified to homogeneity by ion exchange and calmodulin-Sepharose affinity chromatography and electrophoretic elution from preparative sodium dodecyl sulfate-polyacrylamide gels. Antibodies against the 55-kDa CaMBP were raised in sheep and were affinity purified. A 47-kDa high-affinity CaMBP species was demonstrated by limited protease digestion and immunoblot analysis to be derived from the 55-kDa CaMBP. The 55-kDa CaMBP has also been isolated from skeletal muscle. It is not detectable by immunoblot analysis in nonexcitable tissues. Characterization of the 55-kDa high-affinity calmodulin-acceptor protein may further elucidate the role of calcium-calmodulin in the regulation of bioelectricity.
D000818:Animals; D002148:Calmodulin-Binding Proteins / Q000032:analysis*; D002846:Chromatography, Affinity; D004557:Electric Organ / Q000032:analysis; D004593:Electrophorus; D007163:Immunosorbent Techniques; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism
D002148:Calmodulin-Binding Proteins; D010447:Peptide Hydrolases