SEARCH · Search PubMed

Results for “Modifier”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,441 records · Page 80Linked to original sources

PubMed1980

In vitro DNA reaction with a carcinogen: the O,O'-diacetyl-4-hydroxyaminoquinoline 1-oxide changes of stability of modified DNA.

The diacetyl derivative of 4-hydroxyaminoquinoline 1-oxide, the proximate carcinogen of 4-nitroquinoline 1-oxide, was reacted in vitro with native and heat denatured chicken erythrocyte DNA under various conditions. The amount of fixed carcinogen was obtained by using the labeled diacetyl derivative and from this result the molar extinction coefficients of bound carcinogen were calculated in order to allow a direct spectrophotometric determination. A decrease in melting temperature of DNA samples modified by O,O'-diacetyl 4-hydroxyaminoquinoline 1-oxide (di Ac-4HAQO) was measured: the melting temperature depression value is equal to 1.4 degrees C per 1% of modified DNA bases. This result was compared with the values previously obtained by Fuchs and coworkers (Fuchs, R. and Daune, M. (1973) FEBS Lett, 34, 295-298 and Fuchs, R. Lefebvre, J.F., Pouyet, J. and Daune, M. (1976) Biochemistry 15, 3347-3351) for N-acetoxy-N-2-acetylaminofluorene-modified DNA and by Lang et al. [25] for the phenanthrylation of the DNA bases of N-acetoxy-N-2-acetylaminophenanthrene-modified DNA.

Aminoquinolines↗

PubMed1985

Ester-exchange catalyzed by lipase modified with polyethylene glycol.

Lipoprotein lipase was modified with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine; forty-six percent out of seven amino groups in the molecule were substituted. The modified lipase catalyzed ester-exchange reactions between an ester and an alcohol, between an ester and an acid, and between two esters. The modified enzyme catalyzed these reactions not only in organic solvents, but also in straight hydrophobic substrates. As the modified enzyme was extremely stable at elevated temperature, for example at 70 degrees C, this can find many practical applications.

Caproates↗

PubMed1987

Polyethylene glycol derivative-modified cholesterol oxidase soluble and active in benzene.

Cholesterol oxidase from Nocardia sp. was modified with a synthetic copolymer of polyoxyethylene allylmethyldiether (PEG) and maleic acid anhydride (MA anhydride), poly(PEG-MA anhydride). The modified cholesterol oxidase, in which 64% of the amino groups in the protein molecule were coupled to poly(PEG-MA), was soluble in organic solvents and catalyzed the oxidation reaction of cholesterol in benzene to form 4-cholesten-3-one with the enzymic activity of 0.6 mumol/min/mg protein. Using the modified cholesterol oxidase together with polyethylene glycol-modified peroxidase, coupled reactions shown below took place in Cholesterol + O2----4-Cholesten-3-one + H2O2 H2O2 + o-Phenylenediamine----H2O + Oxidized o-Phenylenediamine transparent benzene solution, not in an emulsified system. The oxidation of cholesterol was directly determined in benzene by measuring the absorbance of oxidized o-phenylenediamine at 490 nm.

3-Hydroxysteroid Dehydrogenases↗

PubMed1989

Lipoprotein aggregation as an essential condition of intracellular lipid accumulation caused by modified low density lipoproteins.

We have tested a hypothesis that aggregates of modified low density lipoproteins (LDL) play the key role in the accumulation of lipids by cells of unaffected aortic intima. It was demonstrated using analysis of relative dispersion of light transmission fluctuations as well as gel filtration on Sepharose CL-2B that LDL modified by oxidation, glycosylation, desialylation and malondialdehyde treatment form aggregates under the conditions of culture. Native LDL failed to aggregate under the same conditions. It was demonstrated that modified LDL, unlike native LDL, bring about a 2- to 3-fold rise in cholesteryl ester levels of cultured cells. Moreover, direct and strong correlation (r = 0.86) was observed between the degree of lipoprotein aggregation and the amount of cholesteryl esters accumulated. Removal of modified LDL aggregates by filtration through a 0.1 micron filter or gel filtration completely prevented the intracellular accumulation of cholesteryl esters. These findings indicate that LDL aggregates play an essential, if not the decisive, role in the intracellular accumulation of lipids in vitro.

Aorta↗

PubMed1989

Organic solvents as modifiers of aldrin epoxidase in reconstituted monooxygenase systems and in microsomes.

To examine the response of individual cytochrome P-450 species catalysing the epoxidation of aldrin (Wolff T and Guengerich FP, Biochem Pharmacol 36: 2581-2588, 1987), monooxygenase systems reconstituted from these species were assayed in the presence of 5% (v/v) = 0.87 M ethanol. The activity of cytochromes P-450PB-B and P-450PB-D, two enzymes inducible by phenobarbital was increased seven-fold. The activity of two other P-450 enzymes purified from these animals was either inhibited by 50%, as observed for cytochrome P-450PB-C or remained unchanged, as noted with cytochrome P-450PCN-E. Two P-450 enzymes purified from untreated rats, cytochromes P-450UT-F and P-450UT-H, showed an inhibition by 50 and 20%, respectively, while the activity of cytochrome P-450UT-A was slightly increased by 50%. Indirect evidence that solvents enhance aldrin epoxidation by interacting with the hemoprotein was obtained by the finding that ethanol stimulated the activity of cytochrome P-450PB-B already, before addition of the lipid component, L-alpha-1,2-dilauroyl-sn-glycero-3-phosphocholine. The Km of cytochrome P-450PB-B for NADPH cytochrome P-450 reductase was not altered by ethanol indicating that the interaction between the two enzymes was not affected by the solvent. Other results indicate that the stimulatory solvent binds to a site, apart from the type I or type II binding site. The potency of various hydrophylic solvents to modify aldrin epoxidase activity was assayed in microsomes of rats pretreated with phenobarbital and of untreated male rats. Ethanol, n-propranol, n-butanol, acetone and tetrahydrofuran enhanced enzyme activity of phenobarbital pretreated rats to a maximal extent of two-fold and, at similar concentrations, inhibited the enzyme activity of untreated rats by 50%. The potency of these solvents correlated with their lipophilicity. Methanol and dimethylsulfoxide only slightly modified the activity of induced and noninduced animals. In the presence of 0.5 M n-propranol as the modifying agent, microsomal epoxidase activity of rats pretreated with pregnenolone-16 alpha-carbonitrile, dexamethasone, 3-methylcholanthrene and of control rats was inhibited by 60-80%, whereas the activity of animals pretreated with phenobarbital, DDT, or the polychlorinated biphenyl mixture, Clophen A 50, was stimulated between two- and three-fold. The results reveal that organic solvents frequently used to dissolve monooxygenase substrates may considerably modify the activity of cytochrome P-450 dependent reactions, in particular when purified enzymes are assayed.

1-Propanol↗

PubMed1993

The modified Z-plasty for unilateral cleft lip repair.

In 1965 Davies described a Z-plasty technique for the repair of a unilateral cleft lip. The technique has been modified so that the scars are more aesthetically placed and the orbicularis muscle correctly aligned. A prospective study was performed comparing the results of this modified Z-plasty with the rotation advancement repair. Twelve patients had a modified Z-plasty and 10 a rotation advancement repair. The modified Z-plasty compares favourably with the rotation advancement technique for the repair of a unilateral cleft lip. In particular, the incidence of asymmetry of lip height was greater in the rotation advancement group.

Child↗

PubMed1989

Modification of sialyl residues of glycoconjugates by reductive amination. Characterization of the modified sialic acids.

The sialic acid residues of alpha 1-acid glycoprotein and fetuin were modified by introduction of an amino residue, such as glycine and [3H]glycine. This modification involved (a) the selective periodate oxidation of the exocyclic carbon atoms of the sialic acid residue generating an aldehyde group at C-7, and (b) the reduction of the Schiff base formed with an amino compound by use of sodium cyanoborohydride. Thin layer chromatography, high pressure liquid chromatography, and amino acid composition data of the modified glycoprotein showed that the conversion was essentially quantitative. The glycine-modified sialic acids were isolated by mild acid hydrolysis and identified by g.l.c.-m.s. and n.m.r. spectroscopy, thus confirming that the quantitative modification produced a glycine-aminated C-7 sialic acid analog. Strong acid hydrolysis of the glycine-modified sialic acid yielded a fragment that had chromatographic characteristics similar to those of glycine.

Chemical Phenomena↗

PubMed1984

13C- and 31P-NMR studies of the conformation of carcinogen-modified nucleic acid dimers.

The effect of the carcinogen acetylaminofluorene (AAF) on nucleic acid structure was examined using 13C- and 31P-NMR spectroscopies. Conformational effects were compared in two AAF-modified dinucleoside monophosphates (ApG and GpA) and two AAF-modified deoxydinucleotides (dpApG and dpGpA). Changes in adenine 13C chemical shifts on formation of the AAF-adduct and as a function of temperature provided evidence of base stacking. Differences in fluorene 13C chemical shifts between the AAF-modified dimer and AAF-modified monomer provided evidence of fluorene stacking. The effect of forming the adduct on the phosphate backbone was examined using 31P-NMR. A correlation was demonstrated between the degree of adenine-fluorene stacking on one hand and the change in conformation of the backbone conformation on the other.

2-Acetylaminofluorene↗

PubMed1991

Microtubules rich in post-translationally modified alpha-tubulin form distinct arrays in frog lens epithelial cells.

Isolated frog lens epithelia were stained with antibodies against tyrosinated, detyrosinated or acetylated alpha-tubulin and observed by several means including a scanning confocal microscope. The most prominent feature of Rana pipiens lens cells was a primary cilium close to the apical surface of the cells above the centrosome. This structure was associated with microtubules rich in modified alpha-tubulin. The cilium was less pronounced but still discernible in the cells of another species R. ridibunda. In both species, the modified (acetylated or detyrosinated) microtubules formed arrays spatially distinct from the unmodified (tyrosinated) microtubules. The modified microtubules formed a basket of microtubules with a curly distribution around the nucleus while the tyrosinated array consisted predominantly of rather straighter microtubules running from the apical centrosome to the cell periphery, down the lateral sides of the cells and across the basal surface adjacent to the lens capsule and basement membrane. It is concluded that the organization of modified microtubules previously described for several types of cultured cells may represent a remnant of the three-dimensional perinuclear array of such microtubules described here for the cells of an intact epithelium.

Animals↗

PubMed1990

Factors influencing the formation of modified S2 EPR signal and the S3 EPR signal in Ca(2+)-depleted photosystem II.

NaCl/EGTA-washing of photosystem II (PS-II) results in the removal of Ca2+ and the inhibition of oxygen evolution. Two new EPR signals were observed in such samples: a stable and modified S2 multiline signal and an S3 signal [(1989) Biochemistry 28, 8984-8989]. Here, we report what factors are responsible for the modifications of the S2 signal and the observation of the S3 signal. The following results were obtained. (i) The stable, modified, S2 multiline signal can be induced by the addition of high concentrations of EGTA or citrate to PS-II membranes which are already inhibited by Ca(2+)-depletion. (ii) The carboxylic acids act in the S3-state, are much less effective in S2 and have no effect in the S1-state. (iii) The extrinsic polypeptides (17- and 23-kDa) are not required to observe either the modified S2 signal or the S3 signal. However, they do influence the splitting and the lifetime of the S3 signal, and they seem to have a slight influence on the hyperfine pattern of the S2 signal. (iv) The S3 signal can be observed in Ca(2+)-depleted PS-II which does not exhibit the modified multiline signal. Then, it is proposed that formation of histidine radical during the S2 to S3 transition in Ca(2+)-depleted PS-II [(1990) Nature 347, 303-306] also occurs in functional PS-II.

Calcium↗

PubMed1989

Interaction of pyridoxal phosphate modified cytochromes c with mitoplasts.

1. The stability of the native conformation of the heme crevice of pyridoxal phosphate (PLP)-ferricytochromes c as assayed by the pK, for 695 nm absorption band varies considerably. The pKa values are 8.76 for cytochrome c modified by PLP at lysine 79[PLP(Lys 79)-cyt. c], 9.23 for cytochrome c modified by PLP at lysine 86 [PLP(Lys 86)-cyt.c], 9.34 for doubly PLP substituted cytochrome c at lysines 79 and 86 [(PLP)2-cyt. c], 9.50 for triply substituted cytochrome c [(PLP)3-cyt. c] and 9.06 for native cytochrome c, which indicates less stable heme crevice of PLP-cytochrome c. 2. The singly PLP-modified cytochrome c indicate decreased activities with mitochondrial cytochrome c oxidase in the following order: PLP(Lys 86)-cyt. c less than PLP(Lys 79)-cyt. c less than native cytochrome c. The high affinity Km for PLP(Lys 86)-cyt. c, PLP(Lys 79)-cyt. c and native cytochrome c are 0.28 microM, 0.16 microM and 0.02 microM respectively. 3. PLP-cytochromes c show decreased binding affinities to fluorescence probes 12-(9-antroyl)-stearic acid and pyrene-labelled mitoplasts. The quenching of singly PLP-modified cytochrome c depends significantly on the ionic strength.

Ascorbic Acid↗

PubMed1995

Metabolism of modified LDL by cultured human placental cells.

UNLABELLED: All major classes of normal circulating lipoproteins can be metabolized by human placental cells. However, the metabolism of abnormal or modified lipoproteins has been little studied. We therefore investigated whether placental cells metabolize acetylated low density lipoprotein (ac-LDL) or oxidatively-modified LDL (ox-LDL), both of which are metabolized by scavenger receptors, and if so, whether modified LDL stimulates progesterone secretion as does normal LDL. Placental macrophages and trophoblasts were isolated on a 40% Percoll gradient after enzymatic digestion. The cellular uptake and degradation of [125I]-ac-LDL was 20-fold higher than [125I]-LDL in both macrophages and trophoblasts. Both cell types demonstrated high affinity and saturable degradation. Similarly, increased esterification of [14C]-labelled oleic acid to cholesterol was observed when cells were incubated with ac-LDL vs. LDL. Uptake of ac-LDL by trophoblasts also was demonstrated by colocalization of fluorescently labelled ac-LDL and fluorescent antibodies specific for trophoblasts. Similar colocalization of fluorescent ac-LDL and fluorescent anti-macrophage specific epitopes was seen in macrophages. Uptake and degradation of [125I]-ac-LDL by placental cells was inhibited by increasing concentrations of unlabelled ac-LDL or fucoidin but not LDL, indicating uptake by a scavenger receptor. Both unlabelled ac-LDL and ox-LDL inhibited uptake of [125I]-labelled ox-LDL, suggesting uptake by a common mechanism. Although secretion of progesterone by trophoblasts was stimulated by incubation with LDL, progesterone secretion by trophoblasts was not stimulated by ac-LDL and only minimally stimulated by ox-LDL. CONCLUSIONS: Scavenger receptors are present in human placental trophoblasts as well as macrophages. Scavenger receptor activity greatly exceeds that of LDL receptor activity in both cell types. However, cholesterol assimilated via the scavenger receptor pathway appears to be disconnected from endocrine steroidogenesis in trophoblasts. Thus, we hypothesize that scavenger receptors function in trophoblasts to degrade modified lipoproteins and prevent toxic effects on placental cellular function and fetal growth and development.

Cells, Cultured↗

PubMed1995

Optimization of a modified electrode for the sensitive and selective detection of alpha-dipeptides.

Sensitive and selective detection of dipeptides is important in neurochemistry. We have developed a flexible detection scheme for dipeptides based on a modified carbon electrode. The modification arises from the anodic treatment of the carbon electrode in alkaline solution. The flexibility of the detection scheme arises from the different conditions used in both the modification and the detection. It is shown that the modification step requires the presence of cupric ion, while the detection step does not. On the other hand, it is shown that the presence of copper in the detection eluent, as well as the pH of the environment, can be used in controlling the selectivity of the modified electrode. For example, the modified electrode is more selective for alpha-dipeptides over beta- and gamma-dipeptides as well as amino acids at pH 9.8, whereas it is selective for all dipeptides over amino acids at pH 8.0. Detection limits of dipeptides on the order of 10 nM were achieved at pH 8.0 by flow-injection analysis with a knotted Teflon tubing connecting the injector and the detector that gave a typical peak volume of about 0.50 ml at 1.0 ml/min. From surface analysis it is shown that the oxygenation of the glassy carbon electrode gives rise to the selectivity. The oxidation of dipeptides at the modified electrode is completely inhibited by 10 mM Mg2+ in the eluent.

Chromatography, Liquid↗

PubMed1996

Separation of toxic peptides (microcystins) in capillary electrophoresis, with the aid of organic mobile phase modifiers.

A capillary electrophoretic (CE) method incorporating sodium dodecyl sulphate (SDS)-organic modifier solvents in the CE buffer was developed for the detection of toxic cyclic heptapeptide toxins (microcystins) produced by blue-green algae (cyanobacteria). The applicability of these run buffers for the analysis of microcystins was evaluated and optimum conditions for separation were determined. The migration times, elution order and selectivity of the toxic peptides were influenced by modifying the composition of the electrophoretic buffer with organic solvents [0 to 20% (v/v)]. At maximum addition, the organic solvents with the exception of acetonitrile, increased the viscosity of the buffer solution. In contrast to the migration time of the other microcystins, that of microcystin-RR was not increased by the addition of 2-propanol to the buffer solution. Rather, microcystin-RR eluted more quickly with the increase in 2-propanol, thereby effecting changes in the elution order of the microcystins. In addition, this solvent resulted in comigration of microcystin-LR and microcystin-YR. No significant relationship was found between the elution order and separation and the structure of the toxic peptides studied in micellar electrokinetic capillary chromatography with an organic modifier in the buffer solution; but there is an agreement between the effects of the organic modifiers and their dipole moments. Parameters such as linearity, sensitivity and reproducibility were also evaluated. High-efficiency separations of toxic peptide molecules having equal or nearly equal mass to charge ratios have been achieved using SDS as an additive to the running buffer. The influence of the pH has been examined.

Electrophoresis, Capillary↗

PubMed1994

Clinical evaluation of a modified ELISA, using photobiotinylated DNA, for the detection of anti-DNA antibodies.

The measurement of anti-dsDNA antibodies is important for the diagnosis and the follow-up of patients with systemic lupus erythematosus (SLE). For routine detection of anti-dsDNA, the Farr assay and the immunofluorescence technique (IFT) on Crithidia luciliae proved to be very useful. The anti-dsDNA ELISA is not used for routine purposes in our institute since it is flawed by false-positive results due to binding of negatively charged (immune) complexes to the employed precoat (protamine sulphate). Recently, a new anti-dsDNA ELISA has been described in which photobiotinylated dsDNA is coated to streptavidin coated plates. To investigate whether this modified ELISA is more specific than the classical anti-dsDNA ELISA, we tested sera of patients with SLE (n = 51), myasthenia gravis (MG, n = 25), rheumatoid arthritis (RA, n = 25) and Sjögren's syndrome (SS, n = 23) and sera of healthy blood bank donors (BBD, n = 25). In both assays the sera of the SLE patients gave significantly higher values than the sera of healthy blood bank donors. In the classical ELISA, 84% of the sera from patients with RA and 28% of sera of patients with MG were found positive. For the modified assay the figures were 8% and 24%, respectively. This modified ELISA was further studied and clinically evaluated by comparing it with the classical anti-DNA ELISA and two other anti-DNA assays (Farr assay and IFT), using 500 sera sent to our institute for routine anti-DNA determination and sera of an additional 75 healthy blood bank donors. Quantitatively, both ELISAs showed the same high degree of correlation with the IFT. The modified ELISA gave a better correlation with the Farr assay than the classical anti-DNA ELISA. From our data we conclude that the ELISA using photobiotinylated DNA is a more reliable assay than the classical anti-DNA ELISA.

Antibodies, Antinuclear↗

PubMed1985

A shear test evaluation of a new, modified, unfilled resin.

A shear test was conducted under simulated oral environmental conditions to examine the retention of a new, commercially available modified unfilled resin in comparison with a conventional unfilled resin provided by the same manufacturer. Within the experimental limits of this study no difference was observed between the retention of the conventional and the modified unfilled resins to enamel specimens. However, for dentin specimens the modified resin was clearly superior to the conventional resin, which gave essentially zero retention. With the recommended procedure, the retention of the modified resin to dentin was 13% of that for the retention of either resin to enamel. It was also observed microscopically that the new resin demonstrated good wetting ability of the dentinal surface. The retention of the two resins to dentin with various surface treatments was determined. The recommended surface preparation procedures of cleaning the dentin surface with hydrogen peroxide followed by a water rinse gave equivalent, if not superior, results to a 1-minute etch with phosphoric acid or citric acid followed by a water rinse.

Acid Etching, Dental↗

PubMed1991

Shear resistance of composite resin to enamel using color-modifying resins and variously applied unfilled bonding resins.

The effects of bond layer thickness of color-modifying resins and variously applied unfilled resins on composite resin/enamel shear bond strengths were compared. Composite resin columns were bonded to etched enamel surfaces in vitro with either applied unfilled resins or with filled color-modifying resins. The bond layer thickness and the force required to shear the 17 specimens of each of six groups were measured. ANOVA with Tukey's test was performed to determine if significant differences at the alpha = 0.05 level existed for the mean bond layer thicknesses as well as the mean forces required to debond the specimens of six groups. Color-modifying resins resulted in a 5 to 327 times greater bond thickness than the unfilled resins. Only one of the unfilled resin groups showed a statistically significant difference in shear resistance compared with a color-modifying resin group. The method of application and resulting thickness of unfilled resin appeared to have little effect on composite resin/enamel shear bond strengths.

Acrylates↗

PubMed1983

On the evolution of dominance modifiers I. A nonlinear analysis.

A well known mathematical model of evolution of dominance is subjected to a nonlinear analysis. For the case where the primary locus and the modifying locus are completely linked (r = 0) a global Ljapunov function is given. This proves that selection of dominance modifiers entirely due to their modifying effect is possible. This result is also extended to small recombination fractions r by using the method of Ljapunov functions in a more sophisticated way. For r = 0 and mu = 0 a lower bound for the success of selection of the modifier is given. Furthermore, the influence of the dominance relations between the alleles (measured by the parameters h and k) is investigated. Finally it is shown that differential and difference equations lead to the same results (which need not be the case in general). As a by-product we obtain a new equilibrium point in the classical one locus selection-mutation model.

Alleles↗