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1.
Mutat Res ; 753(1): 41-49, 2013.
Article in English | MEDLINE | ID: mdl-23422071

ABSTRACT

Genetic alterations in cancer tissues may reflect the mutational fingerprint of environmental carcinogens. Here we review the pieces of evidence that support the role of aristolochic acid (AA) in inducing a mutational fingerprint in the tumor suppressor gene TP53 in urothelial carcinomas of the upper urinary tract (UUT). Exposure to AA, a nitrophenathrene carboxylic acid present in certain herbal remedies and in flour prepared from wheat grain contaminated with seeds of Aristolochia clematitis, has been linked to chronic nephropathy and UUT. TP53 mutations in UUT of individuals exposed to AA reveal a unique pattern of mutations characterized by A to T transversions on the non-transcribed strand, which cluster at hotspots rarely mutated in other cancers. This unusual pattern, originally discovered in UUTs from two different populations, one in Taiwan, and one in the Balkans, has been reproduced experimentally by treating mouse cells that harbor human TP53 sequences with AA. The convergence of molecular epidemiological and experimental data establishes a clear causal association between exposure to the human carcinogen AA and UUT. Despite bans on the sale of herbs containing AA, their use continues, raising global public health concern and an urgent need to identify populations at risk.


Subject(s)
Aristolochic Acids/adverse effects , Balkan Nephropathy/genetics , Carcinogens/pharmacology , Mutation/genetics , Tumor Suppressor Protein p53/genetics , Urologic Neoplasms/genetics , Animals , Balkan Nephropathy/chemically induced , Humans , Mice , Urologic Neoplasms/chemically induced
2.
Science ; 157(3784): 84-5, 1967 Jul 07.
Article in English | MEDLINE | ID: mdl-4381747

ABSTRACT

A structural model for the inhibition of protein biosynthesis was previously formulated on the basis of a topochemical analogy between the ipecac alkaloids and the glutarimide antibiotics. The structure of tubulosine satisfies the requirements of this model. The prediction that such a compound would exhibit amebicidal activity and act by selectively inhibiting the transfer reaction in protein biosynthesis is confirmed.


Subject(s)
Alkaloids/pharmacology , Amebicides/pharmacology , Antimetabolites , Protein Biosynthesis , Chemistry, Pharmaceutical , DNA/biosynthesis , Escherichia coli/cytology , HeLa Cells , Hemoglobins/biosynthesis , In Vitro Techniques , Ipecac , Leucine/metabolism , Models, Theoretical , Phenylalanine/metabolism , RNA/biosynthesis , RNA, Transfer/metabolism , Reticulocytes/metabolism , Ribosomes/metabolism , Saccharomyces/cytology
3.
Science ; 174(4005): 159-61, 1971 Oct 08.
Article in English | MEDLINE | ID: mdl-4940963

ABSTRACT

The activity of anthramycin and structurally related analogs as chemosterilants of the housefly, Musca domestica L., correlates closely with the action of these compounds as inhibitors of Escherichia coli RNA polymerase. Since inhibition of RNA polymerase by anthramycin reflects binding of this antibiotic to the DNA primer required for enzyme activity, we propose that the interaction of anthramycin with DNA may also account for its action as a chemosterilant.


Subject(s)
Antibiotics, Antineoplastic/pharmacology , Benzazepines/pharmacology , Chemosterilants/pharmacology , Houseflies/drug effects , Animals , DNA/pharmacology , Drug Interactions , Escherichia coli/enzymology , Female , Male , RNA Nucleotidyltransferases/antagonists & inhibitors
4.
Trends Genet ; 9(7): 246-9, 1993 Jul.
Article in English | MEDLINE | ID: mdl-8379000

ABSTRACT

The presence of reactive oxygen species in cells ensures that the oxidatively damaged base 8-oxoguanine will be generated at high frequency in the DNA of all living organisms. DNA damage threatens genomic integrity: enzymes have evolved that protect prokaryotes and eukaryotes from the mutagenic effect of this ubiquitous lesion.


Subject(s)
DNA Damage , DNA Glycosylases , DNA Repair/physiology , Escherichia coli Proteins , Guanine/analogs & derivatives , Mutagenesis , DNA-Formamidopyrimidine Glycosylase , Escherichia coli/genetics , Guanine/physiology , N-Glycosyl Hydrolases/physiology , Reactive Oxygen Species
5.
Nucleic Acids Res ; 27(24): 4725-33, 1999 Dec 15.
Article in English | MEDLINE | ID: mdl-10572172

ABSTRACT

3,N(4)-Ethano-2'-deoxycytidine (ethano-dC) may be incorporated successfully into synthetic oligodeoxynucleotides by omitting the capping procedure used in the automated DNA synthetic protocols immediately after inserting the lesion and in all iterations thereafter. Ethano-dC is sensitive to acetic anhydride found in the capping reagent, and multiple oligomeric products are formed. These products were identified by examining the reaction of ethano-dC with the capping reagent, and several acetylated, ring-opened products were characterized by electrospray mass spectrometry and collision induced dissociation experiments on a tandem quadrupole mass spectrometer. A scheme for the formation of the acetylated products is proposed. In addition, the mutagenic profile of ethano-dC was re-examined and compared to that for etheno-dC. Ethano-dC is principally a blocking lesion; however, when encountered by the exo(-)Klenow fragment of DNA polymerase, dAMP (22%), TMP (16%), dGMP (5.3%) and dCMP (1.2%) were all incorporated opposite ethano-dC, along with an oligomer containing a one-base deletion (0.6%).


Subject(s)
DNA/chemical synthesis , Oligodeoxyribonucleotides/chemistry , Oligodeoxyribonucleotides/chemical synthesis , Acetylation , Automation , Base Sequence , Chromatography, High Pressure Liquid , DNA/chemistry , DNA Polymerase I/metabolism , Deoxycytidine/analogs & derivatives , Deoxycytidine/pharmacology , Indicators and Reagents , Molecular Structure , Mutagens/chemistry , Mutagens/pharmacology , Spectrometry, Mass, Secondary Ion
6.
Cancer Res ; 56(9): 2130-6, 1996 May 01.
Article in English | MEDLINE | ID: mdl-8616861

ABSTRACT

We analyzed all published deletions and insertions in the p53 gene to assess the relevance of mutagenesis models. Almost all deletions and insertions can be explained by one or more of the following DNA sequence features: monotonic base runs, adjacent or nonadjacent repeats of short tandem sequences, palindromes, and runs of purines or pyrimidines (homocopolymer runs). Increased length of monotonic runs correlates positively with increased frequency of events. Complex frameshift mutations can be explained by the formation of quasi-palindromes, with mismatch excision and replication using one strand of the palindrome as a template. Deletions and insertions in the p53 tumor suppressor gene may reflect both spontaneous and carcinogen-induced mutagenesis.


Subject(s)
Genes, Tumor Suppressor , Models, Genetic , Neoplasms/genetics , Tumor Suppressor Protein p53/genetics , Base Sequence , Gene Deletion , Humans , Molecular Sequence Data , Mutagenesis, Insertional , Neoplasms/metabolism
7.
Cancer Res ; 45(3): 1127-31, 1985 Mar.
Article in English | MEDLINE | ID: mdl-2578872

ABSTRACT

Base propenals arise from DNA by a Fe(II)-bleomycin-mediated reaction which leads to strand scission. These compounds undergo addition-elimination reactions with thiols and other nucleophilic groups under physiological conditions and form an addition product with glutathione. Thymine- and adenine-N1-propenals inhibit DNA synthesis in HeLa cells; both compounds are cytotoxic [50% inhibiting concentration (IC50) = 1 to 2 microM]. A structurally related nucleoside, thymidine-N3-propenal, designed as a metabolic pathway inhibitor, inhibits growth of HeLa, L1210 leukemia, Lewis lung carcinoma, B16 melanoma, and DLD-1 human colon carcinoma cells in culture (IC50 = 1 to 6 microM). A single injection of this compound, administered on the first day following transplant of L1210 leukemia cells, increased the mean survival time of mice by 50% (T/C = 154). Thymidine-N3-propenal selectively blocks DNA synthesis in HeLa cells and inhibits thymidine kinase (Ki = 5.1 microM) and DNA polymerase-alpha. We suggest that base propenals, rather than damaged DNA, account for some of the cytotoxic effects of bleomycin and that nucleoside propenals represent a novel class of site-directed inhibitors.


Subject(s)
Antineoplastic Agents/pharmacology , Bleomycin/pharmacology , DNA, Neoplasm , Thymidine/analogs & derivatives , Thymine/analogs & derivatives , Bleomycin/metabolism , DNA Polymerase II/antagonists & inhibitors , DNA, Neoplasm/metabolism , Glutathione/metabolism , HeLa Cells , Humans , Neoplasm Proteins/biosynthesis , Nucleic Acids/biosynthesis , Thymidine/metabolism , Thymidine/pharmacology , Thymidine Kinase/antagonists & inhibitors , Thymine/pharmacology
8.
Cancer Res ; 60(15): 4098-104, 2000 Aug 01.
Article in English | MEDLINE | ID: mdl-10945616

ABSTRACT

To study the genotoxic properties of 1,N6-ethenodeoxyadenosine (epsilondA) in human cells, a novel site-specific mutagenesis approach was developed, in which a single DNA adduct was uniquely placed in either strand of a shuttle plasmid vector. The analysis of progeny plasmid derived from the modified strand shows that epsilondA, when incorporated into the position of the second A of 5'-CAA (codon 61 of the ras gene), is mutagenic in human cells, inducing A-->T, A-->G, and A-->C mutations. The efficient induction of A-->T transversions in experiments using modified double- and singlestranded DNA substrates supports the hypothesis that A:T-->T:A transversions in human and animal tumors induced by vinyl compounds reflect misinsertion of dAMP opposite this adduct. Mutagenic events were similar when the adduct was incorporated into either the leading or the lagging strand. EpsilondA was more mutagenic than 8-oxodeoxyguanosine, which induced targeted G-->T transversions in HeLa cells. In Escherichia coli, epsilondA did not significantly miscode (<0.27%) even in the presence of induced SOS functions.


Subject(s)
Deoxyadenosines/genetics , Deoxyadenosines/toxicity , Mutagenesis, Site-Directed , Base Sequence , Codon , DNA/chemical synthesis , DNA/drug effects , DNA/genetics , DNA Adducts/genetics , DNA Damage/genetics , Deoxyadenine Nucleotides/genetics , Escherichia coli/genetics , Gene Deletion , Genes, ras/genetics , Genetic Vectors/genetics , HeLa Cells , Humans , Molecular Sequence Data , Transfection , Transformation, Bacterial
9.
Biochim Biophys Acta ; 454(2): 273-84, 1976 Dec 01.
Article in English | MEDLINE | ID: mdl-999905

ABSTRACT

Anguidine, muconomycin A, T-2 toxin, crotocin and trichodermin, a group of 12,13-epoxytrichothecenes, inhibit protein synthesis in HeLa cells and in rabbit reticulocyte lysates. These five mycotoxins can be divided into two groups on the basis of the reversibility of their effects in HeLa cells, and kinetics of inhibition and effects on polyribosome structure in rabbit reticulocyte lysates. Anguidine, muconomycin A and T-2 toxin are irreversible inhibitors of protein synthesis; crotocin and trichodermin are reversible inhibitors of protein synthesis. After addition of low concentrations (1 muM) of anguidine, muconomycin A or T-2 toxin to rabbit reticulocyte lysates, polyribosomes are broken down to monosomes. At higher concentrations, 1 mM, these drugs begin to freeze the polyribosomes. Crotocin and trichodermin freeze the polyribosomes at a concentration of 10 muM. We conclude that anguidine, muconomycin A and T-2 toxin act primarily as inhibitors of initiation of protein synthesis, whereas crotocin and trichodermin inhibit the process of chain elongation.


Subject(s)
Mycotoxins/pharmacology , Protein Biosynthesis , Sesquiterpenes/pharmacology , Trichothecenes/pharmacology , Cell-Free System , DNA/biosynthesis , Globins/biosynthesis , HeLa Cells/drug effects , HeLa Cells/metabolism , Leucine/metabolism , Poly C/metabolism , Poly U/metabolism , Puromycin/metabolism , RNA/biosynthesis , RNA, Transfer/metabolism , Reticulocytes/drug effects , Reticulocytes/metabolism , Ribosomes/metabolism , T-2 Toxin/pharmacology , Thymidine/metabolism , Trichodermin/pharmacology , Uridine/metabolism
10.
J Med Chem ; 29(8): 1329-40, 1986 Aug.
Article in English | MEDLINE | ID: mdl-3525839

ABSTRACT

A series of simple aza and diaza bicyclic quinones related to the AB ring system of streptonigrin (1) have been synthesized and tested in vitro for their ability to degrade DNA under conditions similar to those used with the parent drug. The results obtained from a study of 22 quinones indicate that there is a quantitative linear relationship between their reduction potentials and the rate at which they degrade DNA under identical conditions in vitro. Almost all of the synthetic substances were superior to 1 in their DNA-degrading ability.


Subject(s)
DNA/metabolism , Streptonigrin/analogs & derivatives , DNA, Bacterial/metabolism , Escherichia coli/genetics , Humans , Hydrogen-Ion Concentration , Oxidation-Reduction , Quinones/metabolism , Streptonigrin/pharmacology , Structure-Activity Relationship
11.
J Med Chem ; 27(8): 954-8, 1984 Aug.
Article in English | MEDLINE | ID: mdl-6205151

ABSTRACT

The 1-(3-oxoprop-1-enyl) derivatives of thymine and cytosine and the corresponding 9-substituted derivatives of adenine and guanine (products of degradation of DNA by bleomycin, Fe2+, and O2) have been synthesized and tested for biological activity. The thymine and adenine compounds are highly cytotoxic to a variety of tumor cell lines and inhibit macromolecular synthesis in cultured HeLa cells. Structure-activity studies, based primarily on the pyrimidine derivatives, reveal that the most potent inhibition occurs when the propenal group is located on the 3-nitrogen of a 2'-deoxyribonucleoside. The 3-(3-oxoprop-1-enyl) derivatives of thymidine, 2'-deoxyuridine, and 5-iodo-2'-deoxyuridine powerfully and selectively inhibit incorporation of thymidine into DNA at concentrations (IC50 approximately equal to 0.5 microM) comparable to those observed with idoxuridine. Active compounds in this series react readily with nucleophiles containing primary amino and sulfhydryl groups. The results of this study provide a basis for the development of a new class of cytotoxic agents.


Subject(s)
Antineoplastic Agents/chemical synthesis , Purines/chemical synthesis , Pyrimidines/chemical synthesis , Aldehydes/chemical synthesis , Aldehydes/pharmacology , Cell Survival/drug effects , DNA Replication/drug effects , HeLa Cells/cytology , Humans , Protein Biosynthesis , Purines/pharmacology , Pyrimidines/pharmacology , RNA/biosynthesis , Structure-Activity Relationship
12.
Cancer Lett ; 83(1-2): 315-22, 1994 Aug 15.
Article in English | MEDLINE | ID: mdl-8062231

ABSTRACT

Oligodeoxynucleotides, modified site-specifically with 7,8-dihydro-8-oxodeoxyguanosine (8-oxodG), 7,8-dihydro-8-oxoadenosine (8-oxodA) and 6-O-methyldeoxyguanosine (O6medG), were used as templates for DNA synthesis in primer-extension reactions catalysed by extracts prepared from human (HeLa) cells, simian kidney (COS-7) cells and various mouse tissues. Fully-extended reaction products were analysed by two-phase polyacrylamide gel electrophoresis (Shibutani, Chem. Res. Toxicol. 6, 625, 1993). Using extracts prepared from HeLa or COS-7 cells, dAMP was preferentially incorporated opposite 8-oxodG; dTMP was incorporated opposite 8-oxodA and dTMP, accompanied by small amounts of dCMP, was incorporated opposite O6medG. Translesional synthesis was strongly inhibited by N-ethylmaleimide and partially inhibited by N-butylphenyl-dGTP. This model system can be used to predict the mutagenic potential of selectively-damaged DNA in mammalian cells.


Subject(s)
DNA Damage , DNA Replication , DNA/biosynthesis , Animals , Base Sequence , Chlorocebus aethiops , DNA Polymerase II/antagonists & inhibitors , Deoxyguanine Nucleotides/pharmacology , Ethylmaleimide/pharmacology , Female , HeLa Cells , Humans , In Vitro Techniques , Mice , Mice, Inbred C57BL , Mice, Inbred DBA , Molecular Sequence Data , Mutagenesis , Oligodeoxyribonucleotides/chemistry , Templates, Genetic
13.
Biochem Pharmacol ; 42(2): 431-7, 1991 Jul 05.
Article in English | MEDLINE | ID: mdl-1713460

ABSTRACT

A series of cytotoxic propenal (3-oxoprop-1-enyl) derivatives of pyrimidine bases and deoxynucleosides was evaluated for their ability to block thymidylate synthesis in intact and permeabilized murine leukemia L1210 cells. Several were potent inhibitors of this process, likely contributing to their cytotoxicity. The IC50 values of thymidine-3-propenal, the prototype of this series, in intact and permeabilized L1210, L-M and L-M(TK-) cells were 21, 7.5, and 75 microM and 1.5, 1.7, and 3.5 microM, respectively. The related base analogue, thymine-1-propenal, is a product of bleomycin-induced DNA strand-scission; the results of the present study bear on the mode of action of this antibiotic.


Subject(s)
Acrolein/analogs & derivatives , Deoxyribonucleotides/pharmacology , Leukemia L1210/enzymology , Pyrimidines/pharmacology , Thymidylate Synthase/metabolism , Animals , Bleomycin/metabolism , Cell Line/drug effects , Mice , Mice, Inbred CBA , Thymidine Monophosphate/biosynthesis , Thymidylate Synthase/antagonists & inhibitors , Tumor Cells, Cultured/drug effects
14.
J Am Soc Mass Spectrom ; 11(6): 505-15, 2000 Jun.
Article in English | MEDLINE | ID: mdl-10833024

ABSTRACT

Electrospray mass spectrometry techniques were used to characterize components of the active site in Endonuclease VIII by identifying the amino acid sequence and the binding site for a tryptic peptide derived from Endo VIII in a cross-linked DNA-peptide complex. Endo VIII, a DNA repair enzyme with both glycosylase and lyase activities, was covalently bound to a thymidine glycol-containing oligodeoxynucleotide duplex by converting a transient Schiff base formed during the course of the glycosylase activity to a stable covalent bond by chemical reduction with sodium borohydride. After tryptic digestion of the initial product, the identification of the cross-linked peptide was deduced initially from the molecular mass of the tryptic product obtained by negative ion electrospray mass analysis. Nanospray tandem mass spectrometry (MS/MS) analysis of the tryptic product corroborated the molecular mass of the peptide fragment and verified the point of attachment to the oligomer, but failed to produce sufficient fragmentation to sequence the peptide completely. Direct evidence for the amino acid sequence of the peptide was obtained after enzymatic digestion of the DNA portion of the cross-linked DNA-peptide product and analysis by negative ion nanospray MS/MS. Examination of the ions from collision induced fragmentation disclosed that this substance was the N-terminal tryptic fragment of Endo VIII cross-linked to a portion of the oligomer, and that the N-terminal proline from Endo VIII was covalently bound to the residual deoxyribose moiety at the original location of the thymine glycol in the oligomer.


Subject(s)
DNA Repair , Endodeoxyribonucleases/chemistry , Amino Acid Sequence , Amino Acids/analysis , Binding Sites , Cross-Linking Reagents , DNA/chemistry , Deoxyribonuclease (Pyrimidine Dimer) , Glycols/chemistry , Hydrolysis , Indicators and Reagents , Mass Spectrometry , Molecular Sequence Data , Oligonucleotides/chemistry , Peptides/chemistry , Thymidine/chemistry , Trypsin
15.
Mutat Res ; 376(1-2): 71-8, 1997 May 12.
Article in English | MEDLINE | ID: mdl-9202740

ABSTRACT

The mutagenic properties of 2-acetylaminofluorene-derived DNA adducts, including N-(deoxyguanosin-8-yl)-2-acetylaminofluorene, N-(deoxyguanosin-8-yl)-2-aminofluorene, N-(deoxyguanosin-N2-yl)-2-acetylaminofluorene, and several minor oxidation products have been explored, using site-specific techniques. Oligodeoxynucleotides containing a single AAF-derived DNA adduct were prepared by postsynthetic modification and used as templates in primer extension reactions catalyzed by bacterial and mammalian DNA polymerases. Base substitutions and deletions occurring during DNA synthesis were quantified. dG-C8-AAF promoted one- and two-base deletions and small amounts of incorporation of dCMP, dAMP, and/or dTMP opposite the lesion in reactions catalyzed by the 3'-->5' exonuclease-free Klenow fragment of DNA polymerase 1 (exo-) and polymerase alpha. dG-C8-AF did not miscode in reactions catalyzed by exo-; however, base misincorporation and deletions were observed in reactions with pol alpha. dG-N2-AAF promoted small amounts of dAMP incorporation in reactions catalyzed by exo-. The miscoding potential of minor oxidation products of dG-C8-AF was much higher than that of other adducts. Steady-state kinetics were used to measure frequencies of nucleotide insertion opposite the lesion and chain extension from the 3' terminus. Kinetic data were consistent with the results of primer extension studies. A mutation 'hot spot' was constructed and the influence of sequence context on the frequency of deletions generated by dG-C8-AAF was explored systematically in reactions catalyzed by exo-. Based on our results with aminofluorene DNA adducts, we propose a general mechanism for frameshift deletion mutagenesis. Site-specific methods also were used to establish the mutagenic potential of AAF-derived DNA adducts in mammalian cells. dG-C8-AAF and dG-C8-AF exhibited similar mutagenic specificities, predicting the occurrence of G-->T transversions and G-->A transitions in mammalian cells.


Subject(s)
2-Acetylaminofluorene/toxicity , DNA Adducts , Mutagenesis , Animals , COS Cells , Cells, Cultured , DNA Replication , DNA-Directed DNA Polymerase/metabolism , Mutagenicity Tests , Sequence Deletion
16.
Mutat Res ; 254(3): 281-8, 1991 May.
Article in English | MEDLINE | ID: mdl-2052015

ABSTRACT

We have constructed a gapped plasmid vector in which a single defined lesion is introduced, site-specifically, within a single-strand region. Efficiency of translesional synthesis is determined by the number of colonies recovered following transformation of E. coli. The nucleotide sequence of progeny plasmids in the gapped region of the vector reflects incorporation of bases opposite and near the lesion. The analysis detects non-mutagenic as well as mutagenic events. This system was used to establish the mutagenic potential of 2'-deoxy-7,8-dihydro-8-oxoguanosine (8-oxodG), a lesion produced by the action of active oxygen species on DNA. The presence of 8-oxodG did not affect the number of transformants recovered. Most transformants (greater than 99%) contained G:C pairs at the site of the lesion; however, a limited number of targeted G----T transversions were observed in the presence and absence of SOS induction. Base substitutions neighboring the lesion, reported for an in vitro system, were not observed. We conclude that the 8-oxodG lesion in DNA is weakly mutagenic in E. coli.


Subject(s)
DNA Damage , DNA/drug effects , Deoxyguanosine/analogs & derivatives , Escherichia coli/genetics , Genetic Vectors , Mutagenesis, Site-Directed , 8-Hydroxy-2'-Deoxyguanosine , Base Sequence , DNA/chemistry , Deoxyguanosine/pharmacology , Escherichia coli/drug effects , Molecular Sequence Data , Plasmids , Transformation, Bacterial
17.
Mutat Res ; 407(1): 11-24, 1998 Feb.
Article in English | MEDLINE | ID: mdl-9539977

ABSTRACT

Shuttle plasmid vectors containing the SV40 origin of replication and tandem neo genes with distally placed non-overlapping deletions were used to study the effects of DNA damage on extrachromosomal homologous recombination in simian kidney cells. DNA was introduced into COS7 cells by a lipofectin-mediated transfection procedure and recombination was assessed by analyzing the structure of plasmids. Recombinational events observed included unequal homologous recombination (triplication), gene conversion, double reciprocal recombination, deletion (pop-outs), gene amplification (4-6 copies), and multimerization. Triplication, an event that previously had not been reported in association with extrachromosomal recombination, predominated in experiments with undamaged vectors. The recombination frequency (NeoR/AmpR) of vectors randomly damaged by UV irradiation was essentially unchanged; however, the relative number of triplication events decreased significantly. Selective damage in one of the two neo genes increased the relative frequency of gene conversion. The experimental system developed for use in this study detects all major homologous recombination events observed in chromosomal direct repeat sequences in mammalian cells and yeast and should prove valuable for future studies of homologous recombination in mammalian cells.


Subject(s)
DNA Damage , Gene Conversion , Plasmids/radiation effects , Recombination, Genetic/radiation effects , Ultraviolet Rays , Animals , COS Cells , DNA Replication , Escherichia coli/genetics , Gene Amplification , Gene Deletion , Genes, Viral , Kanamycin Kinase/genetics , Multigene Family , Mutagenesis , Simian virus 40/genetics , Transfection
18.
Adv Exp Med Biol ; 55: 55-70, 1975.
Article in English | MEDLINE | ID: mdl-1155248

ABSTRACT

The binding of alpha- and beta-methyl-D-glucopyranoside and beta-(o-iodo-pheryl)-D-glucopyranoside to concanavalin A has been studied by carbon-13 nuclear magnetic resonance techniques. The kinetics and binding orientations of these saccharides relative to the transition metal ion site in the protein have been determined.


Subject(s)
Concanavalin A , Glucose , Binding Sites , Binding, Competitive , Carbon Isotopes , Chemical Phenomena , Chemistry , Magnetic Resonance Spectroscopy , Manganese , Methylglycosides , Molecular Conformation , Protein Binding , X-Ray Diffraction , Zinc
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