phosphorus-radioisotopes and acetic-anhydride

phosphorus-radioisotopes has been researched along with acetic-anhydride* in 2 studies

Other Studies

2 other study(ies) available for phosphorus-radioisotopes and acetic-anhydride

Article	Year
Adduct formation at C-8 of guanine on in vitro reaction of the ultimate form of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine with 2'-deoxyguanosine and its phosphate esters. Japanese journal of cancer research : Gann, 1992, Volume: 83, Issue:10 We examined the reactivity of the N-hydroxyamino derivative of a carcinogenic heterocyclic amine, 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP), after its O-acetylation with four 2'-deoxyribonucleoside 3'-monophosphates. 32P-Postlabeling analysis demonstrated that the levels of adducts with 2'-deoxyguanosine 3'-monophosphate were much higher than those with the other three nucleotides. 1H-NMR, mass spectral and UV absorption spectral analyses of the major adducts formed by N-acetyoxy-PhIP with 2'-deoxyguanosine and with its phosphate esters indicated that PhIP bound at the C-8 position of guanine, as previously demonstrated with other heterocyclic amines. Topics: Acetic Anhydrides; Biotransformation; Chromatography, High Pressure Liquid; Chromatography, Thin Layer; Cytochrome P-450 Enzyme System; Deoxyguanosine; Guanine; Imidazoles; Isotope Labeling; Magnetic Resonance Spectroscopy; Mutagens; Nucleotides; Phosphates; Phosphorus Radioisotopes; Pyridines; Spectrometry, Mass, Fast Atom Bombardment	1992
Interaction of RNA polymerase II with acetylated nucleosomal core particles. Biochemical and biophysical research communications, 1991, May-31, Volume: 177, Issue:1 Chemical acetylation of nucleosomal cores is accompanied by an increase in their efficiency as in vitro transcription templates. Low amounts of acetic anhydride cause preferential modification of the amino-terminal tails of core histones. Modification of these domains, which causes moderate structural effects, is apparently correlated with the observed stimulation of RNA synthesis. In contrast, extensive modification of the globular regions of core histones, which is accompanied by a large structural relaxation of the particle, causes little additional effect on transcription. Acetylation of the amino-terminal domains of histones might stimulate transcription by changing the interaction of the histone tails with components of the transcriptional machinery. Topics: Acetic Anhydrides; Acetylation; Animals; Chickens; Cytidine Triphosphate; Erythrocytes; Histones; Kinetics; Nucleosomes; Phosphorus Radioisotopes; RNA; RNA Polymerase II; Transcription, Genetic; Uridine Triphosphate	1991

Article

Year

Adduct formation at C-8 of guanine on in vitro reaction of the ultimate form of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine with 2'-deoxyguanosine and its phosphate esters.

Japanese journal of cancer research : Gann, 1992, Volume: 83, Issue:10

We examined the reactivity of the N-hydroxyamino derivative of a carcinogenic heterocyclic amine, 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP), after its O-acetylation with four 2'-deoxyribonucleoside 3'-monophosphates. 32P-Postlabeling analysis demonstrated that the levels of adducts with 2'-deoxyguanosine 3'-monophosphate were much higher than those with the other three nucleotides. 1H-NMR, mass spectral and UV absorption spectral analyses of the major adducts formed by N-acetyoxy-PhIP with 2'-deoxyguanosine and with its phosphate esters indicated that PhIP bound at the C-8 position of guanine, as previously demonstrated with other heterocyclic amines.

Topics: Acetic Anhydrides; Biotransformation; Chromatography, High Pressure Liquid; Chromatography, Thin Layer; Cytochrome P-450 Enzyme System; Deoxyguanosine; Guanine; Imidazoles; Isotope Labeling; Magnetic Resonance Spectroscopy; Mutagens; Nucleotides; Phosphates; Phosphorus Radioisotopes; Pyridines; Spectrometry, Mass, Fast Atom Bombardment

1992

Interaction of RNA polymerase II with acetylated nucleosomal core particles.

Biochemical and biophysical research communications, 1991, May-31, Volume: 177, Issue:1

Chemical acetylation of nucleosomal cores is accompanied by an increase in their efficiency as in vitro transcription templates. Low amounts of acetic anhydride cause preferential modification of the amino-terminal tails of core histones. Modification of these domains, which causes moderate structural effects, is apparently correlated with the observed stimulation of RNA synthesis. In contrast, extensive modification of the globular regions of core histones, which is accompanied by a large structural relaxation of the particle, causes little additional effect on transcription. Acetylation of the amino-terminal domains of histones might stimulate transcription by changing the interaction of the histone tails with components of the transcriptional machinery.

Topics: Acetic Anhydrides; Acetylation; Animals; Chickens; Cytidine Triphosphate; Erythrocytes; Histones; Kinetics; Nucleosomes; Phosphorus Radioisotopes; RNA; RNA Polymerase II; Transcription, Genetic; Uridine Triphosphate

1991