20 research outputs found

    Electron immunohistochemical analysis of localization of neutral Mn2+-dependent DNAase. I. Synthesis of ferritin and colloidal gold conjugates with monospecific antibodies against neutral Mn2+-dependent DNAase | Elektronnoe immunogistokhimicheskoe izuchenie lokalizatsii neitral'noi Mn2+-zavisimoi DNKazy. I. Sintez kon''iugatov monospetsificheskikh antitel k neitral'noi Mn2+-zavisimoi DNKaze s ferritinom i kolloidnym zolotom.

    Get PDF
    Rabbit antibodies against a neutral Mn(2+)-dependent rat liver DNAse were obtained, whose specificity towards DNAse was ascertained by suppression of the enzyme activity both in vitro system and immunoblotting assays. Procedures of synthesis of ferritin and colloidal gold conjugates with antibodies are described. The biological activity of the conjugates proved to be similar to that of the original antibodies

    Properties of deoxyribonuclease of rat liver nuclei and changes in its activity during induced synthesis of nucleic acids

    Get PDF
    DNAase from the proteins of chromatin obtained from rat livers preferentially hydrolyzes denatured DNA on the 3' phosphodiester bonds, forming oligonucleotides consisting of 6 to 8 monomers. The DNAase is not specific with respect to the bases. During the induced synthesis of DNA and RNA in rat liver cells a decrease was noted in the DNAase activity of the chromatin proteins

    Chitinolytic complex of serratia marcescens and peculiarities of its biosynthesis

    Get PDF
    The extracellular chitinolytic complex of Serratia marcescens Bú 211 ATCC 9986 was shown to include three proteins with molecular masses of 58, 52, and 45 kDa (chitinases A, B, and C, respectively). Chitinases A and B were separated from chitinase C and purified from protein admixtures by chromatography on chitin. Chitinase A possessed two isoforms with pI values of 6.25 and 4.85-5.25. Chitinase B had only one isoform with a pI of 4.85-5.25 and appeared to be an endochitinase. In the absence of chitin, the biosynthesis of extracellular chitinases was induced by mitomycin C (MC), an inducer of the SOS-response in cells. In the presence of chitin in the cultivation medium, MC increased the chitinase activity. MC induced the synthesis of all three extracellular chitinases, but not of chitobiase, whose biosynthesis was induced by the substrate. © 1997 MAHK Hayka/Interperiodica Publishing

    Electron immunohistochemical analysis of localization of neutral Mn2+-dependent DNAase. I. Synthesis of ferritin and colloidal gold conjugates with monospecific antibodies against neutral Mn2+-dependent DNAase | Elektronnoe immunogistokhimicheskoe izuchenie lokalizatsii neitral'noi Mn2+-zavisimoi DNKazy. I. Sintez kon''iugatov monospetsificheskikh antitel k neitral'noi Mn2+-zavisimoi DNKaze s ferritinom i kolloidnym zolotom.

    Get PDF
    Rabbit antibodies against a neutral Mn(2+)-dependent rat liver DNAse were obtained, whose specificity towards DNAse was ascertained by suppression of the enzyme activity both in vitro system and immunoblotting assays. Procedures of synthesis of ferritin and colloidal gold conjugates with antibodies are described. The biological activity of the conjugates proved to be similar to that of the original antibodies

    Properties of deoxyribonuclease of rat liver nuclei and changes in its activity during induced synthesis of nucleic acids

    Get PDF
    DNAase from the proteins of chromatin obtained from rat livers preferentially hydrolyzes denatured DNA on the 3' phosphodiester bonds, forming oligonucleotides consisting of 6 to 8 monomers. The DNAase is not specific with respect to the bases. During the induced synthesis of DNA and RNA in rat liver cells a decrease was noted in the DNAase activity of the chromatin proteins

    Properties of deoxyribonuclease of rat liver nuclei and changes in its activity during induced synthesis of nucleic acids

    No full text
    DNAase from the proteins of chromatin obtained from rat livers preferentially hydrolyzes denatured DNA on the 3' phosphodiester bonds, forming oligonucleotides consisting of 6 to 8 monomers. The DNAase is not specific with respect to the bases. During the induced synthesis of DNA and RNA in rat liver cells a decrease was noted in the DNAase activity of the chromatin proteins

    Properties of deoxyribonuclease of rat liver nuclei and changes in its activity during induced synthesis of nucleic acids

    No full text
    DNAase from the proteins of chromatin obtained from rat livers preferentially hydrolyzes denatured DNA on the 3' phosphodiester bonds, forming oligonucleotides consisting of 6 to 8 monomers. The DNAase is not specific with respect to the bases. During the induced synthesis of DNA and RNA in rat liver cells a decrease was noted in the DNAase activity of the chromatin proteins

    Electron immunohistochemical analysis of localization of neutral Mn2+-dependent DNAase. I. Synthesis of ferritin and colloidal gold conjugates with monospecific antibodies against neutral Mn2+-dependent DNAase | Elektronnoe immunogistokhimicheskoe izuchenie lokalizatsii neitral'noi Mn2+-zavisimoi DNKazy. I. Sintez kon''iugatov monospetsificheskikh antitel k neitral'noi Mn2+-zavisimoi DNKaze s ferritinom i kolloidnym zolotom.

    No full text
    Rabbit antibodies against a neutral Mn(2+)-dependent rat liver DNAse were obtained, whose specificity towards DNAse was ascertained by suppression of the enzyme activity both in vitro system and immunoblotting assays. Procedures of synthesis of ferritin and colloidal gold conjugates with antibodies are described. The biological activity of the conjugates proved to be similar to that of the original antibodies

    Chitinolytic complex of serratia marcescens and peculiarities of its biosynthesis

    No full text
    The extracellular chitinolytic complex of Serratia marcescens Bú 211 ATCC 9986 was shown to include three proteins with molecular masses of 58, 52, and 45 kDa (chitinases A, B, and C, respectively). Chitinases A and B were separated from chitinase C and purified from protein admixtures by chromatography on chitin. Chitinase A possessed two isoforms with pI values of 6.25 and 4.85-5.25. Chitinase B had only one isoform with a pI of 4.85-5.25 and appeared to be an endochitinase. In the absence of chitin, the biosynthesis of extracellular chitinases was induced by mitomycin C (MC), an inducer of the SOS-response in cells. In the presence of chitin in the cultivation medium, MC increased the chitinase activity. MC induced the synthesis of all three extracellular chitinases, but not of chitobiase, whose biosynthesis was induced by the substrate. © 1997 MAHK Hayka/Interperiodica Publishing

    Chitinolytic complex of serratia marcescens and peculiarities of its biosynthesis

    No full text
    The extracellular chitinolytic complex of Serratia marcescens Bú 211 ATCC 9986 was shown to include three proteins with molecular masses of 58, 52, and 45 kDa (chitinases A, B, and C, respectively). Chitinases A and B were separated from chitinase C and purified from protein admixtures by chromatography on chitin. Chitinase A possessed two isoforms with pI values of 6.25 and 4.85-5.25. Chitinase B had only one isoform with a pI of 4.85-5.25 and appeared to be an endochitinase. In the absence of chitin, the biosynthesis of extracellular chitinases was induced by mitomycin C (MC), an inducer of the SOS-response in cells. In the presence of chitin in the cultivation medium, MC increased the chitinase activity. MC induced the synthesis of all three extracellular chitinases, but not of chitobiase, whose biosynthesis was induced by the substrate. © 1997 MAHK Hayka/Interperiodica Publishing
    corecore