TY - JOUR
T1 - Purification and partial characterization of two proteinases from Clostridium butyricum M 55
AU - Ciborowski, P.
AU - Hryniewicz, W.
AU - Jeljaszewicz, J.
PY - 1988
Y1 - 1988
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0023993067&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023993067&partnerID=8YFLogxK
U2 - 10.1016/S0176-6724(88)80002-6
DO - 10.1016/S0176-6724(88)80002-6
M3 - Article
C2 - 3293333
AN - SCOPUS:0023993067
SN - 0176-6724
VL - 268
SP - 180
EP - 192
JO - Zentralblatt fur Bakteriologie Mikrobiologie und Hygiene - Abt. 1 Orig. A
JF - Zentralblatt fur Bakteriologie Mikrobiologie und Hygiene - Abt. 1 Orig. A
IS - 2
ER -