[Comparative study of acid SH-dependent proteinases from the swine renal cortex]

The presence of porcine kidney cortex of the SH-dependent enzymes, lysosomal carboxypeptidase B and cathepsins B, H and L, was demonstrated. A method for isolation of these enzymes was described which involves gel filtration through Sephadex G-100, covalent chromatography on mercury-organic Sepharose 4B and rechromatography on Sephadex G-100. Specific activity of lysosomal carboxypeptidase B was increased 9000-fold by BAA splitting and that of cathepsin B 240-fold by BAPA splitting. The molecular weights of lysosomal carboxypeptidase B and cathepsin B were found to be 50,000 and 26,000, respectively. Both enzymes were identical with appropriate enzymes obtained from other sources and differed in their properties from high-molecular-weight SH-proteinase or porcine kidney cortex.