Výsledky vyhledávání - "O V, Khalabuda"

[Dependence of 3'-5-exonuclease activity of a fragment of Klenow DNA polymerase I from Escherichia coli on the length and structure of the cleaved oligonucleotide]

Autor: O V, Khalabuda, G A, Nevinskiĭ, A S, Levina, V V, Gorn, V V, Khomov

Publikováno v: Molekuliarnaia biologiia. 24(5)

The Km and vmax values for oligothymidylates d(pT)2-16 in reaction of 3'-5'-exonuclease hydrolysis catalyzed by Klenow fragment were measured in the absence and presence of poly(dA) template without the poly(dA), the Km values for oligonucleotides ar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e3b1358b9e0bbe8a7e1ce968e3cfd6dd
https://pubmed.ncbi.nlm.nih.gov/1963205

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[Interaction of dNTP-binding sites of human DNA polymerase alpha and The Klenow fragment of Escherichia coli DNA polymerase I with nucleotides, pyrophosphate and their analogs]

Autor: G A, Nevinskiĭ, I A, Potapova, N B, Tarusova, O V, Khalabuda, V V, Khomov

Publikováno v: Molekuliarnaia biologiia. 24(1)

AMP and NaF each taken separately were shown to activate DNA polymerization catalyzed by Klenow fragment of DNA polymerase I by means of interaction of AMP or NaF with 3'----5'-exonuclease center of the enzyme. In the presence of NaF which is a selec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::920ae2c4eb485c1be8383767a9835330
https://pubmed.ncbi.nlm.nih.gov/2161489

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[Purification and characterization of DNA-dependent DNA-polymerase alpha from human placenta]

Autor: O I, Lavrik, G A, Nevinskiĭ, V N, Podust, O V, Khalabuda

Publikováno v: Molekuliarnaia biologiia. 23(2)

A preparation of human placenta DNA polymerase with specific activity 6000 unit/mg was obtained. The protocol of the enzyme purification includes the crude extract preparation, the subsequent chromatographies on phosphocellulose, red sepharose, DEAE

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::53f48aa4c6f536bfb52288559f1aab0e
https://pubmed.ncbi.nlm.nih.gov/2770723

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[Modification of human DNA polymerase alpha by N-acetylimidazole]

Autor: O I, Lavrik, G A, Nevinskiĭ, I A, Potapova, N B, Tarusova, O V, Khalabuda

Publikováno v: Molekuliarnaia biologiia. 23(2)

The modification of tyrosine residues of the human placenta DNA-polymerase alpha by N-acetylimidazole was investigated. The poly(dT)-template and the r(pA)10-primer a each added separately or simultaneously do not influence the rate of enzyme inactiv

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bfcb4fce79bce766953304e3c6b6ae9a
https://pubmed.ncbi.nlm.nih.gov/2549393

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[DNA-polymerase alpha from human placenta. Effectiveness of interaction between oligothymidylates of different lengths and the template-binding site]

Autor: G A, Nevinskiĭ, V N, Podust, A S, Levina, O V, Khalabuda, O I, Lavrik

Publikováno v: Bioorganicheskaia khimiia. 12(3)

Modification of human placenta DNA polymerase alpha by (pT)2pC[Pt2 + (NH3)2OH].(pT)7 was investigated. The linear time dependence of the enzyme activity logarithm suggested a pseudo-first order for modification. Kd value of enzyme-affinity reagent co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3657e47b6ee9fc8d1b7fbf90bfb036d6
https://pubmed.ncbi.nlm.nih.gov/3964308

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