Peroxidase of the common hepatica ( Hepatica nobilis)

An extracition and purification of the peroxicdase from the tissuies of the common hepatica have been carried out. The homogeneity of the extracted catalizator has been proved. The enzyme content was calculated (5,32 mg/ml g/g of the raw tissue). The most important enzymatic parameters of the biocatalizator have been investigated on the course of the multispep methodic and scientific approach for the studying of the catalytic properties of the peroxidase in model systems under the presence of the regulators of the catalytic activity. Values of the most important enzymatic parameters of the catalytic activity of the hepatica peroxidase have been determined: K M = 2.23·10 -3 М, V max = 9,52·10 -3. The results are plausible and correspond to the data from the literature sources.