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V S Vesa

Publications and source records attributed to V S Vesa.

16 recordsLinked to original sources
PubMed1991

[Anti-invasive and anti-metastatic effect of lysine oxidase from Trichoderma sp. in vitro and in vivo].

A new fungal strain, Trichoderma sp., discovered in Moscow, produces the antitumor enzyme, lysine-oxidase, which demonstrates an anti-invasive effect in vitro and anti-metastatic activity in vivo. Maximal inhibition of the in vitro invasion of MM1 clone cells was obtained when the tumor cells were pretreated with 2.5 mU/ml of lysine-oxidase; the pretreatment caused a 1.9-times reduction in cell growth and a 1.6-times reduction in the invasive capacity. We studied its anti-metastatic effect on the spreading Lewis lung carcinoma (3LL) in mice from which the primary tumor had been removed. The administration of the enzyme (50 U/kg, i.v.) significantly decreased not only the extent but the number of lung metastases, as compared with the untreated mice. In addition to that, the lysine-oxidase treatment considerably increases the life-span of mice from which the primary tumor had been removed (200 days after 3LL implantation, lysine-oxidase treatment caused surviving of 50% mice in experimental group).

Amino Acid Oxidoreductases↗
PubMed1984

Trypsin-like enzyme from Streptomyces 771. Purification and properties of native and immobilized enzyme.

Electrophoretically homogeneous proteolytic enzyme with molecular weight 31,500 and pI 3.75 was obtained from a culture medium of Streptomyces 771 by chromatography on N-benzyl chitin adsorbent, subsequent chromatography on CM-cellulose, and preparative isofocusing and chromatography on Sephadex G-75. The enzyme hydrolyzes N-benzoyl-DL-arginine-p-nitroanilide N-benzoyl-DL-lysine-p-nitro-anilide N-benzoyl-DL-arginine ethyl ester, and Na-caseinate. It also exhibits pronounced thrombolytic activity. The activity of the enzyme was suppressed by soya bean inhibitor, but remained unaffected by chelating agents and phenylmethylsulfonyl fluoride. The enzyme was immobilized on aldehyde dextran, and some kinetic parameters of the immobilized enzyme were determined. The thrombolytic activity of native and immobilized enzyme was studied as well.

Amino Acids↗
PubMed1976

[Serine proteases from Bac. subtilis].

Using biospecific adsorbent and subsequent gel-filtration of Sephadex G-75 three fractions of serine proteases (I--III) having different physicochemical properties were isolated from Bac. subtilis. The first protease had molecular weight of 23000--24000 (pH optimum 6,5, activation energy 16,6 ccal/mol. The second one had molecular weight of 29000, pH optimum 11,0, activation energy 14,4 ccal/mol. The third protease was a mixture of proteases with average molecular weights 26000 and pH optima at 7,0, 8,5 and 11,0.

Bacillus subtilis↗
PubMed1976

[Metal proteases from Bac. subtilis].

Metal and serine proteases were separated on the biospecific sorbent. Two different, homogeneous metal proteases were obtained by rechromatography of the metal protease. Activation energies, heat stability, molecular weights, influence of inhibitors, the dependence of activity on pH and temperature were determined. Properties of two metal proteases were compared with those of literary analogs.

Bacillus subtilis↗
PubMedDate not supplied

[Catalytic properties of induced L-lysine-alpha-oxidase].

Regulation of biosynthesis of L-lysine-alpha-oxidase from Trichoderma sp using biostimulators was studied. Specific activity of L-lysine-alpha-oxidase was increased 2.7-fold in presence of biostimulators; this occurred due to induction of the enzyme, properties of which were described previously. Catalytic and physico-chemical properties of the enzyme studied were not altered after addition of stimulators into the cultivation medium of the producing strain. Small amounts of L-lysine-alpha-oxidase isozyme were detected in the medium during cultivation; the isozyme was less active and had lower molecular mass as compared with the enzyme studied.

Amino Acid Oxidoreductases↗
PubMedDate not supplied

[A spectrophotometric method for determining the concentration of L-lysine using L-lysine-alpha-oxidase from Trichoderma sp. and 3,3',5,5'-tetramethylbenzidene dihydrochloride].

A simple and relatively sensitive procedure was developed for determination of L-lysine at 3-30 mmole/L concentration. The procedure does not involve the carcinogenic compound o-dianisidine. L-lysine alpha-oxidase catalyzed oxidative deamination of L-lysine with O2 consumption and formation of H2O2, NH3 and alpha-keto-epsilon-aminocaproic acid. Horseradish peroxidase and a non-carcinogenic compound 3,3,5,5'-tetramethylbenzidine dihydrochloride as an electron donor were used in determination of H2O2 formed. The procedure developed enabled also to measure the L-lysine alpha-oxidase activity at the enzyme concentrations of 10-500 ng/ml. The only limitation of the procedure is relatively low pH-values of the reaction medium.

Amino Acid Oxidoreductases↗
PubMedDate not supplied

[A new method of purification of L-lysine-alpha-oxidase from the fungus Trichoderma].

A new procedure is developed for purification of the antitumoral enzyme L-lysyl-alpha-oxidase from Trichoderma sp. The procedure included two steps: hydrophobic chromatography on butyl sylochrome C-80 and chromatography using biospecific sorbent AH-Sepharose. The simplified procedure enabled to increase distinctly the specific enzymatic activity from 30 to 50 IU/mg in the preparation obtained with a good yield.

Amino Acid Oxidoreductases↗
PubMedDate not supplied

[Improved method of purification of L-lysine-alpha-oxidase from the fungus Trichoderma sp].

Relatively rapid procedure was developed for isolation and purification of the antitumor enzyme L-lysine alpha-oxidase. The procedure involved three steps instead of six or four steps described previously, with a yield of 64.4%. The homogenous preparation was obtained as shown by gel electrophoresis and ultracentrifugation. The antitumor activity of the enzyme both in vivo and in vitro is under investigation.

Amino Acid Oxidoreductases↗
PubMedDate not supplied

[Chromatography of serine proteases on chitin and its derivatives].

Chitin containing sorbents have been obtained for isolation and purification of serine proteases. Serine proteases from Bacillus subtilis have been purified 4-5 times and commercial preparations of trypsin and chymotrypsin 1.5-2 times by chromatography on nondeproteinized chitin. On the benzylated derivative of nondeproteinized chitin complete separation of trypsin and chymotrypsin has been achieved by chromatography of crude pancreatin. It has been shown that the protein moiety of chitin is important for preferential sorption of serine type proteases.

Bacillus subtilis↗
PubMedDate not supplied

[Comparative physico-chemical study of L-lysine-alpha-oxidase from surface and fermenter growth Trichoderma sp].

Homogeneous preparations of L-lysine-alpha-oxidase were obtained from Trichoderma sp cultivated by using a surface technique and a fermenter set. The homogeneous enzyme preparations were similar in molecular mass, isoelectric point and substrate specificity. There was the single difference in the absorbance spectra, which may occur due to the presence of cofactor FAD in various oxidation states. The findings suggest that cultivation of Trichoderma sp in the fermenter set did not alter properties of L-lysine-alpha-oxidase produced.

Amino Acid Oxidoreductases↗