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  • 1
    Electronic Resource
    Electronic Resource
    Time Course of Serum Nuclease Activity in Mice Infected with Plasmodium Malariae (2000)
    Springer
    Bulletin of experimental biology and medicine 130 (2000), S. 877-878 
    Details
    ISSN: 1573-8221
    Keywords: DNase ; RNase ; induction ; Plasmodium malariae ; nonspecific humoral defense
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Time course of DNase and RNase activities in the sera of random-bred mice infected with Plasmodium malariae (chloroquine-sensitive strain H) was studied. Similarly to viral infection, infection with a protozoa eukaryotic parasite was accompanied by increased DNAse and RNAse activities, though Plasmodium malariae biologically differes from viruses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015370429914
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  • 2
    Electronic Resource
    Electronic Resource
    Immobilization of oxyreductases on inorganic supports based on alumina. Immobilization of lactate dehydrogenase on alumina by adsorption (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 23 (1981), S. 1721-1734 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Lactate dehydrogenase (LDH) was adsorbed on low-(γ, η) and high -(θ, α) temperature forms of alumina. θ-Al2O3 exhibited the greatest adsorption ability. The maximum adsorption value was 30 mg LDH/g of a carrier. The conditions for irreversible adsorption have been determined. An adsorption isotherm on θ-Al2O3 for pH 6.0 has been obtained; the LDHads surface area and the carrier surface portion accessible to the enzyme molecules have been calculated. The reaction kinetic parameter were determined by taking into account the reaction proceeding in the intradiffusional region. The specific catalytic activity (Aspec) of LDHads at small surface coverage of θ-Al2O3 is five times less than Aspec of the native enzyme and KMimm with respect to NADH exceeds KMnat by two orders or magnitude. The is evidence for a strong LDH-Al2O3 interaction and a considerable deformation of the enzyme globule. Aspec and KM decrease as the amount of the enzyme attached to the carrier increases. Due to adsorption. LDH becomes thermostable and durable. The LDHads samples conserve 20-40% of their activity at room temperature during a year.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260230805
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  • 3
    Electronic Resource
    Electronic Resource
    Epoxidation of propene by microbial cells immobilized on inorhanic supports (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 522-528 
    Details
    ISSN: 0006-3592
    Keywords: inorganic supports ; gas-utilizing micro-organisms ; adsorption ; double immobuilization ; propene epoxidation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilization of gas-utilizing microorganism strains (Mycobacteria, Rhodococcus, methane-utilizers) on inorganic supports based on alumina, silicates, and carbon was carried out to develop heterogeneous biocatalysts for the biotechnologic processes, including the process of propene epoxidation. Adsorption ability of these microorganisms, biocatalytic properties of resting and immobilized bacterial cells, and effect of immobilization tehniques on biocatalysis were studied. An approach of double immobilization using inorganic materials (supports and gel) was proposed as simple, universal, and available methopd to immobilize bacterial cells, resulting in a higher retention (up to 100%) of cells' enzymatic activity and enhanced stability.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260390507
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  • 4
    Electronic Resource
    Electronic Resource
    Immobilization of oxydoreductases on inorganic supports based on alumina: The role of mutual correspondence of enzyme-support hydrophobic-hydrophilic characters (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 32 (1988), S. 916-919 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260320711
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  • 5
    Electronic Resource
    Electronic Resource
    A novel approach to selective oxidation of gaseous hydrocarbons (1992)
    Springer
    Reaction kinetics and catalysis letters 48 (1992), S. 447-453 
    Details
    ISSN: 1588-2837
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Abstract Процессы селективного окисления углеводородов в мягких условиях можно реализовать при участии микроорганизмов, обладающих монооксигеназной активностью. Исследованы биокаталитические свойства некоторых штаммов метаноотрофов (микроорганизмов, утилизирующих метан в качестве ростового субстрата) в реакциях селективного окисления метана и пропилена. Показано, что в процессе окислительной биотрансформации этих углеводородов при соответствующих условиях и температурах, близких к комнатной, образуются метанол и эпоксид пропилена со 100%-ной селективностью.
    Notes: Abstract Selective oxidation of hydrocarbons can be performed by some microorganisms possessing monooxygenase activity. Biocatalytic activities of some strains of methanotrophic bacteria (which utilize methane as a sole source of carbon and energy for growth) were investigated in the reactions of partial oxidation of methane and propylene. Formation of commercially valuable oxy-products (methanol, epoxide) occurred with 100% selectivity under the mild reaction conditions studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02162693
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  • 6
    Electronic Resource
    Electronic Resource
    A new approach to stabilization of enzymes immobilized on inorganic supports. “Embedded” enzymes (1983)
    Springer
    Reaction kinetics and catalysis letters 22 (1983), S. 125-126 
    Details
    ISSN: 1588-2837
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Abstract Предложен новый принщп стабилизации ферментов на неорчаническнх носителях, заключающийся в “замуровывании” иммобилизованного фермента в порах носителя. На примере алкогольдегидрогеназы показано, что замуровывание иммобилизованного на я-Al2O3 фермента гелем кремневой кислоты резко повышает стабиляностя фермента.
    Notes: Abstract A new approach to the stabilization of enzymes on inorganic supports consisting in the “embedment” of immobilized enzymes in the support pores, is suggested. Exemplified by alcohol dehydrogenase, the “embedment” of the enzyme immobilized on Θ-Al2O3 by silica gel is shown to increase sharply the enzyme stability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02064818
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  • 7
    Electronic Resource
    Electronic Resource
    Adsorption of ε-aminocaproic acid on carbon-containing enterosorbents and antifibrinolytic activity of the immobilized drug (1998)
    Springer
    Pharmaceutical chemistry journal 32 (1998), S. 606-608 
    Details
    ISSN: 1573-9031
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02465836
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  • 8
    Electronic Resource
    Electronic Resource
    Methods for the synthesis of biospecific hemosorbents (1998)
    Springer
    Pharmaceutical chemistry journal 32 (1998), S. 149-153 
    Details
    ISSN: 1573-9031
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02464196
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  • 9
    Electronic Resource
    Electronic Resource
    Immobilized proteolytic enzymes for external use (1998)
    Springer
    Pharmaceutical chemistry journal 32 (1998), S. 213-216 
    Details
    ISSN: 1573-9031
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02464213
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  • 10
    Electronic Resource
    Electronic Resource
    Immobilization of oxyreductases on inorganic supports based on alumina-immobilization of alcohol dehydrogenase on nonmodified and modified alumina (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 3177-3184 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260251228
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