The purification and characterisation of m-calpain from ostrich brain

Int J Biochem Cell Biol. 2002 Apr;34(4):337-47. doi: 10.1016/s1357-2725(01)00139-x.


Calpains are intracellular cysteine proteases activated in a Ca(2+)-dependent manner. The purpose of the present study was to investigate the physico-chemical and kinetic properties of ostrich brain m-calpain. m-Calpain was purified by successive chromatographic steps on Toyopearl-Super Q 650s and Pharmacia Mono Q HR 5/5 columns. A Ca(2+) concentration of 5mM and a casein concentration of 5mg/ml were found to be necessary for optimum calpain activity. Ostrich m-calpain exhibited a M(r) of 84K using SDS-PAGE and a M(min) of 79.3K from amino acid analysis. The pH and temperature optima were found to be 7.5 and 37 degrees C, respectively. The amino acid composition of m-calpain revealed 700 residues. The N-terminal sequence of m-calpain showed sequence identity with chicken (27%), human (23%) and rabbit (18%) and Schistoma mansoni (9%).

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Brain / enzymology*
  • Calcium / metabolism
  • Calpain / chemistry*
  • Calpain / isolation & purification*
  • Calpain / metabolism
  • Caseins / metabolism
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Inhibitors / pharmacology
  • Hemoglobins / metabolism
  • Humans
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Sequence Data
  • Struthioniformes* / anatomy & histology
  • Substrate Specificity
  • Temperature
  • Thermodynamics


  • Caseins
  • Enzyme Inhibitors
  • Hemoglobins
  • azocasein
  • Calpain
  • m-calpain
  • Calcium