Horseradish peroxidase isozyme C. A comparative study of native and recombinant enzyme produced by E. coli transformants.
The purification and refolding of the recombinant horseradish peroxidase produce by E. coli transformants are described. The recombinant enzyme is of 34 kDa and has an isozyme spectrum similar to Sigma type VI horseradish peroxidase. The specific activity of the refolded peroxidase is of about 2000 U/mg with ABTS as a substrate. The recombinant and native enzyme are similar with respect to their catalytic properties in the reaction of enhanced chemiluminescence. Operational and thermal stability of the refolded peroxidase is two to three times lower than for the native one.
Chemistry Department, Lomonosov Moscow University, Russia.
A M
AM
Egorov
I G
IG
Gazaryan
B B
BB
Kim
V V
VV
Doseyeva
J L
JL
Kapeljuch
A N
AN
Veryovkin
V A
VA
Fechina
D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D006735:Horseradish Peroxidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008163:Luminescent Measurements; D008970:Molecular Weight; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014170:Transformation, Genetic
D007527:Isoenzymes; D011994:Recombinant Proteins; D006735:Horseradish Peroxidase