[Purification and properties of recombinant Erwinia carotovora L-asparaginase expressed in E.coli cells].
The method of purification Erwinia carotovora recombinant L-asparaginase, expressed in E.coli, including ultrasonic disintegration of biomass, fractionation ammonium sulfate and column chromatography on CM- or SP-Sepharose has been developed. According to SDS-PAAGE the enzyme preparation was homogeneous, its specific activity and yield consist respectively about 620 IU/mg of protein and 75%. Physical-chemical and structural properties of recombinant Erwinia carotovora L-asparaginase are similar to the enzymes from the wild strains Erwinia carotovora and recombinant L-asparaginase Erwinia chrysanthemi.
Borisova
A A
AA
El'darov
M A
MA
Zhgun
A A
AA
Aleksandrova
S S
SS
Omel'ianiuk
N M
NM
Sokov
B N
BN
Berezov
T T
TT
Sokolov
N N
NN
D001215:Asparaginase / Q000096:biosynthesis / Q000302:isolation & purification*; D002847:Chromatography, Agarose; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D016973:Pectobacterium carotovorum / Q000201:enzymology*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification
D011994:Recombinant Proteins; D001215:Asparaginase