FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2049343760> ?p ?o ?g. }

• W2049343760 endingPage "1041" @default.
• W2049343760 startingPage "1025" @default.
• W2049343760 abstract "Abstract Equilibrium binding is believed to play an important role in directing the subsequent covalent attachment of many carcinogens to DNA. We have utilized UV spectroscopy to examine the non-covalent interactions of aflatoxin B1 and B2 with calf thymus DNA, poly(dAdT):poly(dAdT), and poly(dGdC):poly(dGdC), and have utilized NMR spectroscopy to examine non-covalent interactions of aflatoxin B2 with the oligodeoxynucleotide d(ATGCAT)2. UV-VIS binding isotherms suggest a greater binding affinity for calf thymus DNA and poly(dAdT):poly(dAdT) than for poly(dGdC):poly(dGdC). Scatchard analysis of aflatoxin B1 binding to calf thymus DNA in 0.1 M NaCl buffer indicates that binding of the carcinogen at levels of bound aflatoxin ⁢ 1 carcinogen per 200 base pairs occurs with positive cooperativity. The cooperative binding effect is dependent on the ionic strength of the medium; when the NaCl concentration is reduced to 0.01 M, positive cooperativity is observed at carcinogen levels ⁢ 1 carcinogen per 500 base pairs. The Scatchard data may be fit using a “two-site” binding model [L.S. Rosenberg, M J. Carvlin, and T.R. Krugh, Biochemistry 25, 1002–1008 (1986)]. This model assumes two independent sets of binding sites on the DNA lattice, one a high affinity site which binds the carcinogen with positive cooperativity, the second consisting of lower affinity binding sites to which non-specific binding occurs. NMR analysis of aflatoxin B2 binding to d(ATGCAT)2 indicates that the aflatoxin B2/oligodeoxynucleotide complex is in fast exchange on the NMR time scale. Upfield chemical shifts of 0.1–0.5 ppm are observed for the aflatoxin B2 4-OCH3, H5, and H6a protons. Much smaller chemical shift changes ⁢ 0.06 ppm) are observed for the oligodeoxynucleotide protons. The greatest effect for the oligodeoxynucleotide protons is observed for the adenine H2 protons, located in the minor groove. Nonselective T1 experiments demonstrate a 15–25 % decrease in the relaxation time for the adenine H2 protons when aflatoxin B2 is added to the solution. This result suggests that aflatoxin B2 protons in the bound state may be in close proximity to these protons, providing a source of dipolar relaxation. Further experiments are in progress to probe the nature of the aflatoxin B1 and B2 complexes with polymeric DNA and oligodeoxynucleotides, and to establish the relationship between the non-covalent DNA-carcinogen complexes observed in these experiments, and covalent aflatoxin B1,-guanine N7 DNA adducts." @default.
• W2049343760 created "2016-06-24" @default.
• W2049343760 creator A5018790383 @default.
• W2049343760 creator A5026902410 @default.
• W2049343760 creator A5058755910 @default.
• W2049343760 creator A5059327438 @default.
• W2049343760 date "1988-04-01" @default.
• W2049343760 modified "2023-09-23" @default.
• W2049343760 title "Carcinogen-Nucleic Acid Interactions: Equilibrium Binding Studies of Aflatoxins B₁and B₂with DNA and the Oligodeoxynucleotide d(ATGCAT)₂" @default.
• W2049343760 cites W115941175 @default.
• W2049343760 cites W1595334274 @default.
• W2049343760 cites W1676685876 @default.
• W2049343760 cites W1963725477 @default.
• W2049343760 cites W1968191853 @default.
• W2049343760 cites W1971481046 @default.
• W2049343760 cites W1976540680 @default.
• W2049343760 cites W1978344977 @default.
• W2049343760 cites W1983649348 @default.
• W2049343760 cites W1984996905 @default.
• W2049343760 cites W1985010795 @default.
• W2049343760 cites W1985159559 @default.
• W2049343760 cites W1988882783 @default.
• W2049343760 cites W1989651677 @default.
• W2049343760 cites W1992719829 @default.
• W2049343760 cites W2002155277 @default.
• W2049343760 cites W2002684814 @default.
• W2049343760 cites W2009208424 @default.
• W2049343760 cites W2010576255 @default.
• W2049343760 cites W2013733971 @default.
• W2049343760 cites W2020563452 @default.
• W2049343760 cites W2023202383 @default.
• W2049343760 cites W2026039391 @default.
• W2049343760 cites W2036847094 @default.
• W2049343760 cites W2042838120 @default.
• W2049343760 cites W2046679514 @default.
• W2049343760 cites W2049962121 @default.
• W2049343760 cites W2050586885 @default.
• W2049343760 cites W2053618719 @default.
• W2049343760 cites W2066390300 @default.
• W2049343760 cites W2066703244 @default.
• W2049343760 cites W2080610707 @default.
• W2049343760 cites W2083053197 @default.
• W2049343760 cites W2135399306 @default.
• W2049343760 cites W2168342276 @default.
• W2049343760 cites W2223160714 @default.
• W2049343760 cites W2319015612 @default.
• W2049343760 cites W2483180739 @default.
• W2049343760 doi "https://doi.org/10.1080/07391102.1988.10506447" @default.
• W2049343760 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3152158" @default.
• W2049343760 hasPublicationYear "1988" @default.
• W2049343760 type Work @default.
• W2049343760 sameAs 2049343760 @default.
• W2049343760 citedByCount "22" @default.
• W2049343760 countsByYear W20493437602015 @default.
• W2049343760 countsByYear W20493437602023 @default.
• W2049343760 crossrefType "journal-article" @default.
• W2049343760 hasAuthorship W2049343760A5018790383 @default.
• W2049343760 hasAuthorship W2049343760A5026902410 @default.
• W2049343760 hasAuthorship W2049343760A5058755910 @default.
• W2049343760 hasAuthorship W2049343760A5059327438 @default.
• W2049343760 hasConcept C107824862 @default.
• W2049343760 hasConcept C114246631 @default.
• W2049343760 hasConcept C166014724 @default.
• W2049343760 hasConcept C178790620 @default.
• W2049343760 hasConcept C180577832 @default.
• W2049343760 hasConcept C185592680 @default.
• W2049343760 hasConcept C187250156 @default.
• W2049343760 hasConcept C24107716 @default.
• W2049343760 hasConcept C31903555 @default.
• W2049343760 hasConcept C40758303 @default.
• W2049343760 hasConcept C552990157 @default.
• W2049343760 hasConcept C55493867 @default.
• W2049343760 hasConcept C66974803 @default.
• W2049343760 hasConcept C71240020 @default.
• W2049343760 hasConceptScore W2049343760C107824862 @default.
• W2049343760 hasConceptScore W2049343760C114246631 @default.
• W2049343760 hasConceptScore W2049343760C166014724 @default.
• W2049343760 hasConceptScore W2049343760C178790620 @default.
• W2049343760 hasConceptScore W2049343760C180577832 @default.
• W2049343760 hasConceptScore W2049343760C185592680 @default.
• W2049343760 hasConceptScore W2049343760C187250156 @default.
• W2049343760 hasConceptScore W2049343760C24107716 @default.
• W2049343760 hasConceptScore W2049343760C31903555 @default.
• W2049343760 hasConceptScore W2049343760C40758303 @default.
• W2049343760 hasConceptScore W2049343760C552990157 @default.
• W2049343760 hasConceptScore W2049343760C55493867 @default.
• W2049343760 hasConceptScore W2049343760C66974803 @default.
• W2049343760 hasConceptScore W2049343760C71240020 @default.
• W2049343760 hasIssue "5" @default.
• W2049343760 hasLocation W20493437601 @default.
• W2049343760 hasLocation W20493437602 @default.
• W2049343760 hasOpenAccess W2049343760 @default.
• W2049343760 hasPrimaryLocation W20493437601 @default.
• W2049343760 hasRelatedWork W1004292963 @default.
• W2049343760 hasRelatedWork W1492164242 @default.
• W2049343760 hasRelatedWork W1520771983 @default.
• W2049343760 hasRelatedWork W1534300168 @default.
• W2049343760 hasRelatedWork W1977392864 @default.

• next