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PubMed2002

Involvement of plasma-membrane NADPH oxidase in abscisic acid- and water stress-induced antioxidant defense in leaves of maize seedlings.

The roles of the plasma-membrane (PM) NADPH oxidase in abscisic acid (ABA)- and water stress-induced antioxidant defense were investigated in leaves of maize ( Zea mays L.) seedlings. Treatment by exogenous ABA (100 micro M ABA) or osmotic stress (-0.7 MPa induced by polyethylene glycol) significantly increased the activity of the PM NADPH oxidase, the production of leaf O(2)(-), the activities of several antioxidant enzymes (superoxide dismutase, catalase, ascorbate peroxidase and glutathione reductase), and the contents of antioxidant metabolites (ascorbate and reduced glutathione). Pretreatment with three different inhibitors of NADPH oxidase (diphenylene iodonium, imidazole and pyridine) or an inhibitor of ABA biosynthesis (tungstate) reduced the increase in the activity of the PM NADPH oxidase and the production of leaf O(2)(-), and the capacity of antioxidant defense systems mediated by ABA. The inhibitory effects above caused by tungstate were reversed by exogenous ABA. These data indicate that NADPH oxidase is involved in the ABA-induced production of active oxygen species (AOS), and our results depict a minimal chain of events initiated by water stress-induced ABA accumulation, which then triggers the production of AOS by membrane-bound NADPH oxidase, resulting in the induction of antioxidant defense systems against oxidative damage in plants.

Abscisic Acid↗
PubMed2005

Enhancing effect of calcium and vanadium ions on thermal stability of bromoperoxidase from Corallina pilulifera.

Bromoperoxidase from the macro-alga Corallina pilulifera is an enzyme that possesses vanadate in the catalytic center, and shows a significant thermostability and stability toward organic solvents. The structural analysis of the recombinant enzyme overexpressed in yeast revealed that it contains one calcium atom per subunit. This has been confirmed by inductively coupled plasma emission spectrometry experiments. The study of the effect of metal ions on the apo-enzyme stability has shown that the calcium ion significantly increased the enzyme stability. In addition, vanadate also increased the thermostability and strontium and magnesium ions had similar effects as calcium. The holo-enzyme shows high stability in a range of organic solvents. The effect of the different ions and solvents on the structure of the enzyme has been studied by circular dichroism experiments. The high stability of the enzyme in the presence of organic solvents is useful for its application as a biocatalyst.

Amino Acid Sequence↗
PubMed1997

Effectiveness of diamond-impregnated felt wheels for polishing a hybrid composite.

The effectiveness of diamond-impregnated felt wheels for polishing the surfaces of a fine-particle hybrid composite was studied in relation to different finishing methods. Standardised composite specimens were finished with one or a series of two or three finishing diamonds (particle size 30, 15 and 8 microns), one or two tungsten carbide finishing burs (12- and 30-fluted) or with a finishing diamond followed by a tungsten carbide bur. The final polishing of all specimens was done with the diamond-impregnated felt wheel Diafix alpha. Treatment with Sof-Lex discs after the use of a finishing diamond served as a polishing standard for comparison. Evaluation of the final surfaces was done with profilometry and by scanning electron microscopy. The profilometric results showed that the type of pretreatment was decisive for the quality of the final polishing. Nearly all surfaces polished by the diamond-impregnated felt wheels were smoother than those treated by the flexible discs (P < 0.01). The lowest roughness data were recorded following a pretreatment with a finishing diamond and a tungsten carbide finishing bur. After appropriate pretreatment, the hybrid composite surface was sufficiently polished with the diamond-impregnated felt wheels.

Analysis of Variance↗
PubMed1985

On the chemical basis of the Lowry protein determination.

The copper-catalyzed oxidation of peptides and proteins by phosphomolybdic/phosphotungstic acid (Folin phenol reagent) was studied with respect to redox stoichiometry of color formation and nature of the oxidation products. From peptides without reducing side chains two reducing equivalents were transferred under ideal conditions to Mo6+/W6+ for each unit of tetradentate copper complex with concomitant formation of an imino peptide. Tyrosine and tryptophan side chains contributed four additional reducing equivalents. Oxidation of proline-containing peptides was greatly impaired as judged from color formation due to the interference of the imino acid with complex formation. Reaction of the oxidized peptides with 2,4-dinitrophenyl (DNP)-hydrazine gave a peptide amine and the DNP-hydrazone of a 2-oxoacyl peptide. The oxidation products from tetraalanine were identified as dialanine amide and pyruvoylalanine DNP-hydrazone. From the time course of the development of the blue color on reduction of Folin reagent with tetraalanine it was inferred that the reaction consisted of an initial (less than 5 s) oxidation to a Cu3+ peptide complex followed by slow changes in absorbance, especially above 0.2 mM. Due to these complications the two-electron stoichiometry has to be considered only as a limiting case for peptide concentrations below 0.02 mM.

Chemical Phenomena↗
PubMed1986

Determination of proteins and sulfobetaine with the Folin-phenol reagent.

This paper describes a method for the quantitative analysis of solutions containing a mixture of proteins and sulfobetaine. In a preliminary step the proteins, which interfere with the detergent assay, are separated by precipitation with trichloroacetic acid (8%). The insoluble fraction, dissolved in NaOH (1.0 N), and the soluble fraction, containing the detergent, are treated with the Folin-Ciocalteu phenol reagent, essentially following the method of O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall (1951, J. Biol. Chem. 193, 265-275). The absorbance of the protein fraction is read, as usual at 750 nm, while that of the detergent solution is read at 342 nm. At this wavelength, sulfobetaine, treated with the Folin reagent, absorbs strongly, the absorbances being proportional to its concentration up to 1.5 mg/ml.

Betaine↗
PubMed1987

Fiftyfold amplification of the Lowry protein assay.

The blue product of the Lowry et al. (1951, J. Biol. Chem. 193, 265-275) reaction interacts with malachite green (MG), inducing a change in the visible light spectrum. At A690 nm the absorbance of malachite green solutions increases 10-fold in the presence of Lowry blue (LB). Under the optimum conditions, 0.01 A700 nm unit of Lowry blue produces a change in A690 nm unit of malachite green of 0.5 and the delta A690 nm is a linear function of Lowry blue concentration. Conditions under which this 50-fold amplification can be exploited to detect less than 100 ng of protein (or 4 micrograms X ml-1) are described. A number of chemicals including sodium dodecyl sulfate can interfere with the assay but a strategy has been devised to overcome these problems. Amplification of the Lowry assay appears to involve a cooperative interaction between malachite green and the Lowry blue product such that about 23 molecules of malachite green undergo a spectral shift per molecule of a model reactant such as tyrosine. Malachite green can be used to amplify the molybdenum blue signal obtained in other assays. Less than 10 pmol of tyrosine can be detected using this procedure. Lowry blue also interacts with auramine O, giving a large increase in A500 nm and a 40-fold amplification of the LB signal. As with malachite green, there is a cooperative interaction between auramine O and LB. About 72 molecules of auramine O undergo a spectral shift per molecule of tyrosine. The product of this reaction is also fluorescent and could be exploited in a protein assay.(ABSTRACT TRUNCATED AT 250 WORDS)

Benzophenoneidum↗
PubMed1990

Lowry protein assay containing sodium dodecyl sulfate in microtiter plates for protein determinations on fractions from brain tissue.

A modified Lowry protein assay which contains sodium dodecyl sulfate (Markwell et al., 1978, Anal. Biochem. 87, 207-210) has been adapted for use in 96-well microtiter plates. A spectrophotometer interfaced with a computer is used to plot the standard curve and calculate the protein content of each sample. The method is suitable for measuring 4-40 micrograms of protein/assay in a volume of 50 microliters. There was no need for prior solubilization of proteins which had been extracted from brain tissue. Test samples, up to 21 in triplicate, can be tested on a single microtiter plate plus standards. Alternatively, further samples can be tested separately on extra plates using the standard curve from the original plate for calculations.

Alzheimer Disease↗
PubMed1992

A model for formulation of protein assay.

The principle of the protein assay using the reaction of an alkaline copper-protein complex with the Folin-Ciocalteu phenol reagent has been investigated. In contrast to the long-established Lowry method, a stable and rapid protein assay is developed without a buffering agent in alkaline copper solution. In the absence of a buffering agent, the reaction pH drops relatively rapidly and moves the reaction toward a more stable pH. When the reaction of alkaline copper-protein complex with Folin-Ciocalteu reagent is started at around pH 11.7, the reaction color absorbance reaches a plateau in approximately 10 min and remains stable to allow a reliable measurement of the absorbance. In the absence of the buffering agent sodium carbonate, the alkaline copper solution is also stable for months. The principle of the protein assay is presented as a model that can be used to formulate protein assays of desired specification.

Colorimetry↗
PubMed1984

Effects of electron mediator charge properties on the reaction kinetics of hydrogenase from Chlamydomonas.

Anions modulate hydrogenase activity in cell-free preparations of Chlamydomonas reinhardtii, and this modulation is greatly influenced by the charge properties of the redox agent included to mediate electron transfer to hydrogenase. With cationic methyl viologen as the electron mediator, anions stimulate the maximum velocity of H2 production (e.g., a 320% increase in the presence of 1 M NaCl) but have little effect on the Km for methyl viologen. Conversely, when hydrogenase activity is mediated by polyanionic metatungstate or ferredoxin, H2 production is strongly inhibited by anions (e.g., 70-77% inhibition by 0.2 M NaCl). This inhibition is primarily due to a reduced affinity of hydrogenase for these mediators (as evidenced by a large increase in Km values), rather than a change in the maximum velocity of the reaction. Anions have little effect on the kinetics of hydrogenase activity mediated by zwitterionic sulfonatopropyl viologen, a redox agent with a nearly neutral net charge. These results suggest the presence of a cationic region near the active site of hydrogenase. This cationic region, probably due to lysine and/or arginine residues, may serve in vivo to facilitate the interaction between hydrogenase and ferredoxin, the polyanionic, physiological electron mediator.

Anions↗
PubMed1980

Tungsten-induced inactivation of molybdoenzymes in Anabaena.

The effect of tungsten on growth and activity of two molybdoenzymes has been studied in a nitrogen-fixing heterocystous cyanobacterium, Anabaena. Sodium tungstate inhibited growth and inactivated nitrogenase and nitrate reductase. The activity of both enzymes was restored by the addition of molybdenum. Tungstate treatment caused increase in heterocyst frequency both in NO3- medium and in medium free of combined nitrogen. These results suggest that tungstate treatment inactivates the molybdoenzymes in this cyanobacterium.

Cyanobacteria↗