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G F Denisova

Publications and source records attributed to G F Denisova.

4 recordsLinked to original sources
PubMed1976

[A proteolytic enzyme bound to the aspartate transaminase of swine heart cytosol].

Purified preparations of aspartate transaminase from pig heart cytosol contain a tightly bound proteolytic enzyme (approximately 2, 5%). The enzyme was separated from aspartate transaminase by gel-filtration on Sephadex G-100 in the presence of sodium dodecyl sulfate and by affinity chromatography on the column with Sepharose, containing covalently bound denaturated aspartate transaminase. Protease has a pH optimum of 9.0 and molecular weight of about 23.000-25.000. The proteolysis rates of different subforms of aspartate transaminase depend on their denaturation lability. A more stable choloenzyme is split at a slower rate than the apoenzyme. An enriched preparation of protease was also shown to split glutamate decarboxylase from E. coli and had no effect on cysteinlyase from hen egg, as well as on lactate dehydrogenase and albumin.

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PubMedDate not supplied

[Native and artificial sub-forms of cytoplasmic aspartate transaminase from swine heart].

Multiple forms of aspartate transaminase from cytosol of pig heart (alpha, beta and psi) were incubated in 0.05 M acetate buffer, pH 5.0 at 4 degrees within 5 and 8 months. Gradual accumulation of denaturated forms was observed on incubation of alpha- and beta-forms; these forms possessed higher mobility in polyacrylamide gel disc electrophoresis and decreased enzymatic activity as compared with the native forms. Multiple forms, produced during ageing of alpha-form, were separated by chromatography on CM-cellulose. Chromatographic resolution of the forms, their activity and spectral properties suggest that they are not identical with the native isoenzymes found in the cell.

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PubMedDate not supplied

[The antigenic and immunogenic properties of a recombinant protein of the HIV-1 gag-pol gene secreted by Saccharomyces cerevisiae yeast cells].

Analysis of the immunological properties of recombinant proteins of HIV-1 gene gag-pol secreted by yeast cells S. cerevisiae was carried out. The proteins under study interacted with antibodies from HIV-1-seropositive human subjects and with antibodies of rabbit immune serum to the native virus as effectively and specifically as natural HIV-1 proteins. The yeast gag-pol-protein complex was markedly immunogenic and induced in animals synthesis of antibodies of a certain specificity spectrum. A comparative immunochemical analysis of the properties of the recombinant proteins carried out by EIA and immune blot showed a certain degree of similarity between the yeast proteins and those of analogous construction produced in E. coli system.

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