Publications by authors named "L P Malynovs'ka"

Serological properties of fructosobisphosphatases (FBPases) of Bacillus subtilis 668 and PGD agent of cereals--the mollicute Acholplasma laidlawii var. granulum st. 118 (Alg 118) were studied in a comparative aspect with the help of the reaction of double diffusion in gel according to Ouchterlony.

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Molecular weight of extracellular fructosobisphosphatase of Acholeplasma laidlawii var. granulum strain 118--an agent of pale-green dwarf of cereals has been determined. This enzyme is the basic factor of pathogenicity of this organism, and, maybe, of all phytoplasmas, owing to realization of the enzyme noncontrolled function in the plant organism, its habit acquires the disease symptoms characteristic of "yellows".

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The reactions of glycolysis or gluconeogenesis proceed in good coordination in the cells of microorganisms, and each stage of these processes is distinctly regulated. Under such conditions fructose-bisphosphatase (FBPase) activity (the enzyme level being constant in the cells of microorganisms) is inhibited by adenosine-5'-monophosphate (AMP) and is activated by phosphoenolpyruvate (PEP) depending on the kind of the source of carbon (glycolytic or glyconeogenic) used for microorganism growth. It is evident that the corresponding regulation of FBPase should be absent in the extracellular environment where one cannot observe a distinct coordination of functioning of the enzyme systems.

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The influence of 16 substances-effectors on the extracellular mollicute fructosobisphosphatase (FBPhase) was studied for the first time. These effectors are used, as a rule, when studying properties of this enzyme biopreparations newly isolated from the cells of animals, plants and cells of microorganisms. It was established that optimum pH for FBPhase of mollicutes is whithin 7.

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Amino acid assimilation by different representatives of Acholeplasma genus has been investigated. It was shown that all 7 investigated typical strains Acholeplasma laidlawii PG-8, A. granularum BTS-39, A.

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