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[Bacterial L-asparaginase and glutamin(asparagin)ase: some properties, structure and anti-tumor activity].
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Experimental material on structurally and functional organization, regulation of biosynthesis and activity, mechanism of action, genetic determinants, heterologous expression of bacterial L-asparaginases is accumulated. The modern approaches to isolation and purification of these enzymes, some
[Molecular and biochemical principles of neoplasm enzyme therapy].
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Bacterial enzymes are antineoplastic perspective agents in oncology. Current strategy of tumor enzyme therapy is primarily based on the strictly defined differences of biochemical properties between normal and tumor cells and more precisely on their different sensitivity to deficit of essential
[Inactivation of microbial glutamin-(asparagin-)ase by azaserine and 6-diazo-5-oxo-L-norleucine].
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The effect of substrate analogues on glutamin-(asparagin-)ase from Pseudomonas aurantiaca-548 has been studied. The enzyme was demonstrated to be highly sensitive to the the action of 6-diazo-5-oxo-L-norleucine and azaserine. L-isomers of glutamine, aspartate, glutamate and several other substrate
[Biological properties of L-asparaginase preparations from E. coli in cell cultures].
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Non-specific cytotoxicity and specific antitumor activity of 5 preparations of L-asparaginase from E. coli were studied. Two cell line, i.e. the asparagine-dependent (Berkitt lymphoma cells) and asparagin-independent (human ovary cancer cells) were used as the test-system. Incorporation of
[Cellular test system for studying the biological properties of preparations with L-asparaginase activity].
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L-Asparaginase sensitivity and asparagin-deficiency of 5 tumor cell populations, i.e. mouse lymphoma L-1210, LI0-1, LTL, Berkitt lymphoma and human ovary cancer, line CaOv were studied. Radiometric estimation of 3H-thimidine incorporation into the cells of DNA served a criterion of cytotoxicity.
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