Biomedical subjects

I V Ulezlo

Publications and source records attributed to I V Ulezlo.

22 records · Page 2Linked to original sources

PubMedDate not supplied

[Purification of glucosoisomerase from Lactobacillus brevis and its physico-chemical properties].

Glucosoisomerase isolated from disrupted cells of Lactobacillus brevis 74 by extraction with K, Na phosphate buffer was purified by step-by-step fractionation with (NH4)2SO4 and DEAE-cellulose chromatography. The purified enzyme was examined by polyacrylamide gel electrophoresis and ultracentrifugation. The examination showed the enzyme to be homogeneous. The sedimentation constant of the enzyme was found to be 8.3 S. The molecular weight of the enzyme was estimated to be 200 000. The presence of the carbohydrate moiety in the enzyme was demonstrated by qualitative methods.

Aldose-Ketose Isomerases↗

PubMedDate not supplied

[Highly purified glucosoisomerase from Actinomyces olivocinereus 154].

The paper presents a method for producing highly purified glucosoisomerase from Actinomyces olivocinereus 154. The scheme of purification includes enzyme extraction from dry biomass, acetone fractionation, ammonium sulfate precicipation, and Sephadex G-200 chromatography. The highly purified enzyme is homogeneous as shown by polyacryl amide gel electrophoresis, analytical ultracentrifugation, and gel filtration. The highly purified enzyme has been prepared in a crystalline form. The molecular weight of the enzyme has been estimated by sedimentation equilibrium to be 162 000 and by gel filtration to be 158 000. The sedimentation constant of glucosoisomerase has been found to be 8.52 S.

Actinomyces↗

PubMedDate not supplied

[Conversion of D-glucose into D-fructose in a column reactor with immobilized glucose isomerase].

Conversion of D-glucose into D-fructose in a column reactor of a continuous type was studied using an immobilized enzyme, glucose isomerase from Actinomyces olivocinereus. The effective parameters of Km, Vmax, energy activation at various flow rates were calculated. During 32 days of continuous operation the enzyme activity fell down to 84% of the initial level. A system of recirculation was employed to use immobilized glucose isomerase with a low activity.

Actinomyces↗

PubMedDate not supplied

[Study of oxidative enzymes of the lignin-degrading fungus Pleurotus ostreatus].

The elctrophoretic separation in polyacrylamide gel of laccase and peroxidase isoenzymes of the lignin-degrading fungus Pleurotus ostreatus was investigated. The optimal electrophoretic conditions were found: in the electrode buffer tris-diethyl barbituric acid pH 7.0 in the gradient gel-4-10% acrylamide. Seven peroxidase isoenzymes oxidizing base benzidine and guaiacol were identified and five laccase isoenzymes reacting with specific substrates-p-phenylene diamine, alphs-naphthol, pyrogallol, hydroquinone were determined.

Agaricales↗