[Alkaline extracellular proteinase from Bacillus intermedius. Isolation, purification, and some properties of the enzyme].
Extracellular alkaline proteinase was isolated from the Bacillus intermedius culture medium. The enzyme was purified by ion-exchange chromatography 200-fold to apparent homogeneity and has a specific activity of 950 u./mg. The proteinase was maximally active at pH 10, 50 degrees C and is stable at pH 6.3-11.0. EDTA, o-phenanthroline or p-chloromercuribenzoate did not affect the enzyme activity, while phenylmethylsulfonyl fluoride inhibited it by 95-97%. It was concluded that the enzyme is subtilisin-like and belongs to the serine proteinase family of Bacilli.
Balaban
N P
NP
Sharipova
M R
MR
Usmanova
A M
AM
Itskovich
E L
EL
Leshchinskaia
I B
IB
D001407:Bacillus / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis
D003470:Culture Media; D010450:Endopeptidases
Shchelochnaia vnekleochnaia proteinaza Bacillus intermedius. Vydelenie, ochistka i nekotorye svoĭstva fermenta.