Purification and characterization of a calsequestrin-like calcium-binding protein from carp (Cyprinus carpio) sarcoplasmic reticulum

Abstract

1. A calsequestrin-like calcium-binding protein was purified from carp sarcoplasmic reticulum by column chromatographies using DEAE-cellulose and Butyl-Toyopearl 650S. 2. The mol. wt was estimated to be 50 kDa, which was larger than that of rabbit calsequestrin (42 kDa). 3. Carp calsequestrin-like protein bound Ca2+ with a higher affinity (apparent Kd = 400 microM) and lower capacity (25 mol/mol) compared with rabbit calsequestrin (1 mM and 40-50 mol/mol, respectively). 4. Anti-carp calsequestrin-like protein rabbit antiserum reacted with rabbit calsequestrin in immunoblotting analysis. 5. Carp calsequestrin-like protein was rich in acidic amino acids, as was rabbit calsequestrin.