Purification and partial characterization of two proteinases from Clostridium butyricum M 55

P. Ciborowski, W. Hryniewicz, J. Jeljaszewicz

Research output: Contribution to journalArticle

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Abstract

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 languageEnglish (US)
Pages (from-to)180-192
Number of pages13
JournalZentralblatt fur Bakteriologie Mikrobiologie und Hygiene - Abt. 1 Orig. A
Volume268
Issue number2
DOIs
StatePublished - Jan 1 1988

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Clostridium butyricum
Peptide Hydrolases
DEAE-Cellulose Chromatography
Enzymes
Osmolar Concentration
Polyacrylamide Gel Electrophoresis
Ethanol
Metals
Ions
Amino Acids
Temperature
Proteins

ASJC Scopus subject areas

  • Immunology

Cite this

Purification and partial characterization of two proteinases from Clostridium butyricum M 55. / Ciborowski, P.; Hryniewicz, W.; Jeljaszewicz, J.

In: Zentralblatt fur Bakteriologie Mikrobiologie und Hygiene - Abt. 1 Orig. A, Vol. 268, No. 2, 01.01.1988, p. 180-192.

Research output: Contribution to journalArticle

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