Purification and partial characterization of two proteinases from Clostridium butyricum M 55.
Clostridium butyricum M55 proteinases were purified by application of a multistep procedure involving ethanol precipitation, DEAE cellulose chromatography and molecular sieving. The purified enzymes obtained were called proteinase I and proteinase II. They appeared to be homogeneous when examined by molecular sieving and polyacrylamide gel electrophoresis. The highly purified proteinases were studied for their physico-chemical properties. The influences of pH, temperature, ionic strength and amino acids composition were investigated. The effects of metal ions and of protein-structure-modifying agents support views suggesting the character of these enzymes.
Ciborowski
P
P
Department of Bacteriology, National Institute of Hygiene, Warsaw, Poland.
Hryniewicz
W
W
Jeljaszewicz
J
J
D000596:Amino Acids / Q000032:analysis; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003013:Clostridium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000032:analysis / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013696:Temperature
D000596:Amino Acids; D010450:Endopeptidases