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I F Nes

Publications and source records attributed to I F Nes.

At least 91 records · Page 5Linked to original sources
PubMed1988

Isolation and identification of mutagens from a fried Norwegian meat product.

Two samples of a typical Norwegian minced meat emulsion were fried at 215 degrees C. One had the regular composition while 4.2% creatine was added to the second sample prior to frying. Mutagens in both samples were purified using aqueous acid extraction, XAD-2 adsorption and a series of semipreparative and analytical high performance liquid chromatography (HPLC) purification steps monitored by the Ames/Salmonella mutagenicity test. Mutagenic activity in the creatine-fortified product was enhanced 15-fold. Mutagenicity profiles from reverse-phase and normal-phase HPLC were qualitatively similar for both samples indicating no major production of new mutagens due to the presence of additional creatine. A total of 8 distinct mutagenic peaks could be separated after three additional HPLC steps. These compounds fall into a class of compounds called amino-imidazoazaarenes (AIA). The majority of mutagenic activity is made up by the known cooking mutagens 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline (MeIQx), 2-amino-3,4,8-trimethylimidazo[4,5-f]quinoxaline (DiMeIQx), 2-amino-3-methylimidazo[3,5-f]quinoline (IQ) and 2-amino-n,n,n-trimethylimidazopyridine (TMIP). Smaller contributions are from 2-amino-3-methylimidazo- [4,5-f]quinoxaline (IQx), 2-amino-n,n-dimethylimidazopyridine (DMIP), 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) and two oxygen-containing AIA. With respect to mass, MeIQx and PhIP were the dominating mutagens.

Chromatography, High Pressure Liquid↗
PubMed1988

Inhibitory mechanisms of Maillard reaction products.

In order to determine the inhibitory mechanism of antibacterial Maillard reaction products (MRP), heated mixtures containing arginine and xylose (AX) or histidine and glucose (HG) were studied for their mutagenic effect, using the Salmonella mutagenic test system ('Ames test'), with regard to their effect on the uptake of serine, glucose and oxygen and for their effect on iron solubility. It was found that the MRPs tested had little or no mutagenic effect, while an inhibitory effect on the uptake of serine, glucose and oxygen was observed. The MRPs also had an effect on the solubility of iron in nutrient broth and in phosphate buffer. While the AX mixture reduced the solubility of iron it was increased by the HG mixture. The reduction of iron solubility in the presence of the AX mixture was much greater at pH 8 than at pH 5. The present data suggest that the antibacterial effect of the MRPs tested is primarily due to the interaction between MRPs and iron, resulting in reduced oxygen uptake.

Arginine↗
PubMed1986

Mutagen formation in fried meat emulsion containing various amounts of creatine.

The formation of mutagens in fried, minced meat emulsion was evaluated by the Ames Salmonella test system. Exogenous addition of creatine to the emulsion prior to frying greatly enhanced the mutagenicity of the emulsion. Addition of 5% creatine resulted in a 40-fold increase in the mutagenicity of the fried meat emulsion in the frameshift test strain, TA98, and in a 8-fold increase in the base substitution test strain, TA100. The present results suggest that creatine is an important factor in the mutagen formation in fried meat products.

Cooking↗
PubMed1983

The effect of parabens on DNA, RNA and protein synthesis in Escherichia coli and Bacillus subtilis.

The effect of methyl, propyl and butyl esters of p-hydroxybenzoic acid on DNA and RNA synthesis has been tested in toluenized cells of Escherichia coli and Bacillus subtilis. Both RNA and DNA synthesis of these bacteria were inhibited. The inhibitory concentrations were higher than those previously reported for growth inhibition. Protein synthesis in cell-free extracts (S-30 fraction) of B. subtilis was even more sensitive to parabens than DNA and RNA synthesis, while protein synthesis in Esch. coli was largely unaffected.

Bacillus subtilis↗
PubMed1981

Effect of ATP on the Friend Murine leukemia virus-associated endonuclease activity and the endonuclease activity of the avian myeloblastosis virus RNA-directed DNA polymerase.

The Mn2+-dependent endonuclease activity associated with the avian myeloblastosis virus RNA-directed DNA polymerase has been shown to be activated by ATP in the presence of Mg2+. In the presence of Mn2+ the endonucleolytic activity was stimulated about 3-fold by the addition of ATP. The earlier identified Mr = 40,000 Friend murine leukemia virus (F-MuLV)-associated endonuclease which functions in the presence of both Mg2+ and Mn2+ has also been shown to be similarly stimulated by ATP. For both endonuclease activities stimulation was only observed at ATP concentrations above 0.5 mM, and it did not increase upon elevating the ATP concentration above 2.5 mM. ADP and dATP also stimulated both activities, although not to the same extent as ATP. GTP had no apparent effect and AMP seemed to inhibit both activities. The effect ATP analogs had on the F-MuLV associated endonuclease activity could suggest that the endonuclease reaction in the presence of ATP might involve the cleavage of beta-gamma phosphate bonds in ATP. Neither adenyl-5'-yl imidodiphosphate nor (beta, gamma-methylene)adenosine 5'-triphosphate stimulated the activity, whereas significant stimulation was observed in the presence of (alpha, beta-methylene)adenosine 5'-triphosphate. Although no ATPase activity could be detected in the purified F-MuLV endonuclease preparation, the data do not exclude the possibility that ATP may be cleaved in amounts which are equivalent to the number of nicks introduced into DNA by the virus-associated endonuclease. In the presence of ATP and Mg2+ the F-MuLV-associated endonuclease nicked both supercoiled and linear DNA duplexes extensively, although the former was nicked more readily than the latter. Single-stranded DNA functioned poorly as a substrate. The nicks introduced by the enzyme contained a 5'-phosphoryl terminus and a 3'-hydroxyl group.

Adenosine Triphosphate↗
PubMed1981

Purification and properties of 3-methyladenine-DNA glycosylase from L-cells.

3-Methyladenine-DNA glycosylase from L-cells has been purified approximately 800-fold. The enzyme is present primarily in the nucleus of the cells. The enzymatic reaction was sensitive to changes in the assay conditions and optimum activity was found at pH 6.5 and at 100 mM KCl. Mg2+ did not effect the enzymatic reaction, which also worked in the presence of EDTA. The activity on denatured methylated DNA was 20-40% of that of the native double-stranded form. Sephadex gel filtration of the most purified fraction revealed enzyme species with molecular weights of 68000, 47000 and 27000, which differ from those reported for corresponding enzymes from other organisms. Addition of the product, 3-methyladenine, to the reaction mixture resulted in inhibition of the glycosylase activity of up to 60%. The remaining activity could not be abolished by increasing the concentration of 3-methyladenine.

Adenine↗
PubMed1981

Effect of polyamines on enzymes involved in DNA repair.

The influence of polyamines on various enzymes involved in the excision repair pathway of DNA, such as UV endonuclease, DNA polymerase I, DNA ligase and polynucleotide kinase, and two AP-endonucleases, were studied. The polymerizing activities of DNA polymerase I and polynucleotide kinase were found to be markedly affected by polyamines. In the former enzyme the effect can be attributed to the stabilization of the correct bihelical structure at the 3' end and in the latter case polyamines stabilize the polynucleotide kinase protein itself in the correct oligomeric structure. The effect of polyamines on the hydrolysis of apurinic and apyrimidinic sites in DNA and nucleosome particles were also investigated. Spermine and spermidine were found to be the most efficient polyamines in causing such hydrolysis both in the free DNA and in the nucleosome particles.

Animals↗
PubMed1980

Purification and properties of DNA endonucleases associated with Friend leukemia virus.

An endonuclease associated with the core of Friend leukemia virus (FLV) has been purified more than 10(3)-fold by ion exchange chromatography and gel filtration. Its molecular weight was determined by gel filtration to be about 40,000. Divalent cations were required for the endonuclease to function and KCl concentrations above 50 mM inhibited the enzyme activity. In the presence of Mg++ the purified enzyme nicked preferentially supercoiled circular DNA duplexes and in most of these molecules only one single-stranded nick was introduced per strand. The regions into which the nick could be introduced appeared to be randomly distributed on the circular molecule. When Mn++ was substituted for Mg++ the number of nicks introduced into DNA by the purified enzyme was greatly increased, and both relaxed circular and linear DNA duplexes were nicked as well as supercoiled circular DNA duplexes. Prior to its purification, however, in the presence of Mn++ the endonuclease activity in the virus extract was able to differentiate between circular and linear DNA duplexes, since both supercoiled and relaxed circular duplexes were nicked much more readily than linear duplexes. Single-stranded DNA functioned poorly as a substrate for the purified enzyme.

Cell Line↗
PubMed1980

Characterization of an endonuclease activity associated with Friend-murine leukemia virus.

An endonuclease activity shown to be associated with Friend leukemia virus has been characterized using double-stranded phi X174 DNA as substrate. In the presence of Mg2+, the endonuclease activity was able to convert supercoiled circular DNA duplexes to the relaxed form by introducing single-stranded nicks into the DNA. Most of the nicked DNA duplexes contained only one nick per strand, since unit length DNA was the predominant species obtained when the nicked DNA was analyzed by alkaline sucrose gradient centrifugation. The regions into which the nick could be introduced were evenly distributed around the circular DNA molecule. When Mn2+ was substituted for Mg2+ in the reaction mixture, the number of nicks introduced into circular DNA duplexes by the virus associated endonuclease was greatly increased. In contrast to circular duplexes, linear duplexes and single-stranded DNA functioned poorly as substrates for the virus-associated enzyme. The Friend leukemia virus-associated endonuclease activity is with respect to these characteristics very similar to the endonuclease activity associated with the p32 protein of the avian myeloblastosis virus [1]. The molecular weight of the Friend leukemia virus endonuclease was estimated by gel filtration on a Sephacryl S-200 column to be about 45 000.

Chromatography, Gel↗
PubMed1980

Purification and characterization of an endonuclease specific for apurinic sites in DNA from a permanently established mouse plasmacytoma cell line.

An endonuclease specific for apurinic sites in double stranded DNA has been purified 373-fold from the nuclei of mouse plasmacytoma cells (line MPC-11). The enzyme is free of any detectable amounts of aspecific nucleases. The enzyme does not act on methylated or OsO4-treated DNA. However, high doses of UV-light and gamma-rays render the DNA slightly susceptible to endonucleolytic attack, which is believed to be due to depurination of depyrimidination caused by the treatment. The molecular weight of the enzyme is determined to be 28,000 and its apparent Km of the purified enzyme is calculated to be 2.7 nM apurinic sites. The activity is not absolutely dependent upon the presence of Mg2+ in the assay mixture although metal chelating agents such as sodium citrate and EDTA abolish the activity completely. The nuclease was stimulated by moderate concentrations of potassium chloride optimizing at 50 mM, and higher concentrations inhibiting the activity. The pH optimun for the reaction was 9.5.

Animals↗
PubMed1980

Purification and properties of a mouse-cell DNA-repair endonuclease, which recognizes lesions in DNA induced by ultraviolet light, depurination, gamma-rays, and OsO4 treatment.

A DNA-repair endonuclease has been purified 117-fold from mouse plasmacytoma cells (line MPC-11) by gel filtration, followed by ion-exchange and affinity chromatography. Its molecular weight was determined by gel filtration to be 28,000 +/- 2000. The enzyme recognizes apurinic and apyrimidinic sites induced by acid and gamma-rays in DNA, as well as another type of lesion(s) which is introduced into DNA by both ultraviolet irradiation and OsO4. Quantitative measurements of the number of nicks the purified DNA-repair endonuclease makes in DNA treated with various amounts of OsO4 and ultraviolet light suggests that the endonuclease may act on 5,6-dihydroxydihydrothymine lesions. The endonuclease activity was sensitive to the ionic strength and was most active in the presence of 100 mM KCl, whereas the presence of divalent cations did not stimulate the activity.

Animals↗
PubMed1978

Endonuclease activities from a permanently established mouse cell line that act upon DNA damaged by ultraviolet light, acid and osmium tetroxide.

The activity of damage-dependent endonuclease in mouse plasmacytoma cells (line MPC-11) has been studied using damaged phi X 174 RFI DNA as substrate. The DNA was treated with ultraviolet light, acid, or osmium tetroxide to introduce different types of lesions. Ultraviolet light-damaged DNA was cleaved at approx. 1.1 sites per 35 thymine-containing dimers by the extract, which indicates no specificity towards this type of lesion. The acid-treated DNA, which contains apurinic sites, was enzymatically broken in every alkalilabile site and this strongly suggests the presence of an apurinic-specific endonuclease activity in the nuclear extract. The activity which acts on ultraviolet-irradiated DNA and that which acts on acid-treated DNA have different specificities as shown by their salt requirements and the extent to which they are stimulated by magnesium. While the ultraviolet-endonuclease activity was very little affected by reducing the KCl concentration, the apurinic-specific activity was almost completely abolished. Osmium tetroxide renders the DNA an excellent substrate for endonucleolytic activity in the mouse cell extract. The response to KCl and MgCl2 of the osmium tetroxide-specific endonuclease activity is qualitatively similar to that of the endonuclease activity, which acts on ultraviolet-irradiated DNA. Treatment of DNA with osmium tetroxide is known to produce 5,6-dihydroxydihydrothymine which is a minor photoproduct in DNA after irradiation, suggesting that the ultraviolet-specific endonuclease activity acts upon this lesion.

Acetates↗
PubMed1976

Iodination as a probe for small regions of disrupted secondary structure in double-stranded DNAs.

Conditions were established where the thallium-catalyzed iodination of random coil DNA proceeded 100-200 times faster than for native DNA. This reaction was explored as a probe for localized regions of disrupted base pairs in duplex DNA. A heteroduplex was constructed between DNA fragments produced by Hind II + III cleavage of phi80 plac DNA and phi80 plac DNA containing the Ll deletion (73 nucleotides in length). This heteroduplex incorporated twelve times as much iodine as the parent homoduplex fragments. Hence the technique could reveal the presence of a few (two or more) nonpaired cytosines, if they existed within an otherwise helical DNA fragment 789 base pairs long. Iodination studies were performed on superhelical SV40 DNA and on linear lambdaplac DNA. Analysis of the relative amount of iodine in restriction endonuclease fragments of these DNA's revealed the absence of localized single-stranded regions.

Coliphages↗