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 homogenous 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.
|Original language||English (US)|
|Number of pages||13|
|Journal||Zentralblatt fur Bakteriologie Mikrobiologie und Hygiene - Abt. 1 Orig. A|
|State||Published - Jan 1 1988|
ASJC Scopus subject areas