Isolation and characterisation of cathepsin-B from bovine pancreas.

ABSTRACT

Α simple procedure for the isolation of cathepsin B from bovine pan creas employing ammonium sulphate fractionation, DEAE cellulose chromatography and Sephadex G 200 gel filtration is described. The purified enzyme gave a single band on polyacrylamide gel electrophoresis. The molecular weight as determined by gel filtration of the enzyme was 26,850. Its Km and Vmax values were 12·8 mM and 0·303 μmol/min/mg, respectively. The Ki for iodoacetamide was 0·16 mM.