[Isolation and various properties of the lytic enzyme preparation from Streptomyces griseus]. / Poluchenie i nekotorye svoistva liticheskogo fermentnogo preparata iz Streptomyces griseus.

Certain optimal parameters were determined for production of a pure enzyme preparation of the GIOx type from S. griseus by precipitating the enzymes from concentrated fermentation broth filtrate. Antibacterial spectrum of the preparation is comparatively narrow. Still, it showed high lytic activity against streptococci and staphylococci. Investigation of the preparation with the electrofocusing technique revealed that the main lysing component was a protein fraction with its isoelectric point within 8-10.5.

[Preparative variant of the purification of a trypsin-like thrombolytic enzyme from Actinomyces 771]. / Preparativnaia skhema ochistki tripsinopodobnogo tromboliticheskogo fermenta iz Actinomyces 771]

A simple large-scale purification scheme for a trypsin-like enzyme from Actinomyces 771 was developed using carboxylic cation exchange resin Soloze K and DEAE-cellulose. The electrophoretically homogeneous enzyme with the specific trypsin activity of 1.4 U/mg was obtained with a yield of 53%.

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.

[Serine proteases from Bac. subtilis]. / Serinovye proteazy Bacillus 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.

[Metal proteases from Bac. subtilis]. / Metalloproteazy 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.