[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.
D000818:Animals; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000302:isolation & purification; D002401:Cathepsin B; D056655:Cathepsin H; D002403:Cathepsins / Q000302:isolation & purification; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000302:isolation & purification*; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007672:Kidney Cortex / Q000201:enzymology*; D008722:Methods; D013438:Sulfhydryl Compounds / Q000494:pharmacology; D013552:Swine
D013438:Sulfhydryl Compounds; D002268:Carboxypeptidases; D002403:Cathepsins; D010450:Endopeptidases; D043424:Carboxypeptidase B; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; D056655:Cathepsin H
Sravnitel'noe issledovanie kislykh SH-zavisimykh proteinaz iz korkovogo sloia pochek svin'i.