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PubMed2002

Simple PVC-PPy electrode for pH measurement and titrations.

Cobaltabis(dicarbollide) [3,3'-Co(1,2-C2B9H11)](-)-doped polypyrrole (PPy) films have been prepared galvanostatically on glassy carbon electrodes in acetonitrile solution. The potential response behavior of the film of this new material has been investigated in some common pH buffers and in acid-base titrations. The potentiometric characteristics of the resulting films are indicative of a quasi-Nernstian response (approximately 50 mV/pH unit), a linearity range from pH 12 to 3 and correlation coefficients (r2) of approximately 0.98. The electrode is suitable for pH measurements and for monoprotic titrations of strong alkalis with strong acids, and weak bases with strong acids, but the long response time hinders the use of this electrode for multiprotic titrations. The time response has been dramatically improved by reducing the film thickness by using the template effect of a non-conducting polymer (PVC) cast over the graphite surface before PPy deposition. PPy polymerization occurs in the free channels of PVC leading to the formation of PPy wires. The morphological change of PPy does not affect the slope or linearity range. The response of the PVC-PPy electrochemical sensor is rapid and the sensor is easy to prepare, at low cost, and its performance is comparable with that of commercial glass electrodes.

Journal Article↗
PubMed2002

An on-line potentiometric sequential injection titration process analyser for the determination of acetic acid.

An on-line potentiometric sequential injection titration process analyser for the determination of acetic acid is proposed. A solution of 0.1 mol L(-1) sodium chloride is used as carrier. Titration is achieved by aspirating acetic acid samples between two strong base-zone volumes into a holding coil and by channelling the stack of well-defined zones with flow reversal through a reaction coil to a potentiometric sensor where the peak widths were measured. A linear relationship between peak width and logarithm of the acid concentration was obtained in the range 1-9 g/100 mL. Vinegar samples were analysed without any sample pre-treatment. The method has a relative standard deviation of 0.4% with a sample frequency of 28 samples per hour. The results revealed good agreement between the proposed sequential injection and an automated batch titration method.

Acetic Acid↗
PubMed2004

Estimation of uncertainty in pKa values determined by potentiometric titration.

A procedure is presented for estimation of uncertainty in measurement of the pK(a) of a weak acid by potentiometric titration. The procedure is based on the ISO GUM. The core of the procedure is a mathematical model that involves 40 input parameters. A novel approach is used for taking into account the purity of the acid, the impurities are not treated as inert compounds only, their possible acidic dissociation is also taken into account. Application to an example of practical pK(a) determination is presented. Altogether 67 different sources of uncertainty are identified and quantified within the example. The relative importance of different uncertainty sources is discussed. The most important source of uncertainty (with the experimental set-up of the example) is the uncertainty of pH measurement followed by the accuracy of the burette and the uncertainty of weighing. The procedure gives uncertainty separately for each point of the titration curve. The uncertainty depends on the amount of titrant added, being lowest in the central part of the titration curve. The possibilities of reducing the uncertainty and interpreting the drift of the pK(a) values obtained from the same curve are discussed.

Acids↗
PubMed2005

FIA acid-base titrations with a new flow-through pH detector.

A pH-sensitive detector for flow-through potentiometry based on a graphite/quinhydrone composite electrode was applied for flow-injection analysis (FIA) titrations. Hydrochloric acid and acetic acid were titrated by injection of samples into a sodium hydroxide carrier solution. System conditions were optimised by variation of flow rate, injection volume and titrant concentration. The parameters sampling frequency, residence time and dispersion coefficient were determined. The evaluation of peak width (time between the two inflection points on each side of the peak), peak area and slope of the raising edge of the peak lead were studied with respect to their use for calibration. Hydrochloric acid and acetic acid could be titrated down to a concentration of 2 x 10(-4) mol L(-1) using 150-microL injection volumes, which is almost ten times lower than can be achieved using colour indicators and a spectrophotometric detection.

Acetic Acid↗
PubMed2006

Upper airway surgery: the effect on nasal continuous positive airway pressure titration on obstructive sleep apnea patients.

The objective of this study was to observe the change in CPAP pressure after nasal and/or tonsil surgery in a retrospective study involving 17 patients unable to tolerate CPAP titration. All patients had two polysomnography studies for titration: one before and another subsequent to upper airway surgical treatment. The results showed a mean age of 49 +/- 9 years, a body mass index of 30 +/- 4 kg/m(2) and an apnea-hypopnea index of 38 +/- 19. Surgical procedures were radiofrequency reduction of the inferior turbinate (eight patients), septoplasty (one patient), septoplasty with inferior turbinectomy (two patients), septoplasty with inferior turbinate submucosal diathermy (two patients), septoplasty with tonsillectomy (two patients), septoplasty with inferior turbinate submucosal diathermy and tonsillectomy (one patient) and tonsillectomy (one patient). CPAP titration before and after surgery had respectively a mean pressure of 12.4 +/- 2.5 and 10.2 +/- 2.2 cmH(2)O ( P = 0.001). Maximum CPAP pressure was 16.4 cmH(2)O before and 13 cmH(2)O after surgery. A pressure reduction > or =1 cmH(2)O occurred in 76.5% of the patients and > or =3 cmH(2)O in 41.1%. Upper airway surgical treatment appears to have some benefit by reducing nasal CPAP pressure levels. The effect seems to be greater when the prior pressure was > or =14 cmH(2)O.

Adult↗
PubMed2004

Determination of reduction potential of an engineered Cu(A) azurin by cyclic voltammetry and spectrochemical titrations.

The reduction potentials of an engineered CuA azurin in its native and thermally denatured states have been determined using cyclic voltammetry and spectrochemical titrations. Using a 4,4'-dipyridyl disulfide modified gold electrode, the reduction potentials of native and thermally denatured CuA azurin are the same within the experimental error (422 +/- 5 and 425 +/- 5 mV vs. NHE, respectively, in 50 mM ammonium acetate buffer, pH 5.1, 300 mM NaCl, 25 degrees C), indicating that the potential is that of a nonnative state. In contrast, using a didodecyldimethylammonium bromide (DDAB) film-pyrolytic graphite edge (PGE) electrode, the reduction potentials of native and thermally denatured CuA azurin have been determined to be 271 +/- 7 mV (50 mM ammonium acetate buffer, pH 5.1, 4 degrees C) and 420 +/- 1 mV (50 mM ammonium acetate buffer, pH 5.1, 25 degrees C), respectively. Spectroscopic redox titration using [Ru(NH3)5Py]2+ resulted in a reduction potential (254+/-4 mV) (50 mM ammonium acetate buffer, pH 5.1, 4 degrees C) similar to the value obtained using the DDAB film-PGE electrochemical method. Complete reoxidation of [Ru(NH3)5Py]2+-reduced CuA azurin is also consistent with the conclusion that this spectrochemical titration method using [Ru(NH3)5Py]2+ measures the reduction potential of native CuA azurin.

Azurin↗
PubMed1992

The active site titration of proteinases by using alpha 2-macroglobulin and high-performance liquid chromatography.

The active site titration for various proteinases relies on the development of optimal enzyme titrants for each proteinase, but these titrants are only available for a limited number of proteinases. We have described a new active site titration method applicable to various kinds of endoproteinases using small quantities of the enzymes. This method was carried out by using alpha 2-macroglobulin (alpha 2M) as a titrant and a high-performance liquid chromatography (HPLC) system. When the proteinase solution was treated with alpha 2M, the active proteinase was trapped by alpha 2M. In this reaction alpha 2M does not usually complex with inactive proteinase. After the reaction of proteinase with an excess of alpha 2M, the reaction mixture is applied to an HPLC gel column to separate the uncomplexed enzyme from the one complexed with alpha 2M. The active proteinase is complexed and eluted with alpha 2M, but the inactive proteinase is eluted at the original elution volume. The same amount of the enzyme was also applied to the column. From the decrease of the peak height at the elution position of the uncomplexed proteinase, we can estimate the ratio between enzymatically active proteinases and total proteinases. To test the usefulness of this method, we applied this method to chymotrypsin and trypsin whose activities were predetermined by conventional active site titration, and there was good agreement between both results. With this new method, we can estimate a proteinase activity with as little as 200 ng of the enzyme, a very small amount compared with those required in conventional methods.(ABSTRACT TRUNCATED AT 250 WORDS)

Binding Sites↗
PubMed1976

Oxido-reductive titrations of cytochrome c oxidase followed by EPR spectroscopy.

Experiments are described on oxido-reductive titrations of cytochrome c oxidase as followed by low-temperature EPR and reflectance spectroscopy. The reductants were cytochrome c or NADH and the oxidant ferricyanide. Experiments were conducted in the presence and absence of either cytochrome c or carbon monoxide, or both. An attempt is made to provide a complete quantitative balance of the changes observed in the major EPR signals. During reduction, the maximal quantity of heme represented in the high-spin ferric heme signals (g approximately 6; 2) is 25% of the total heme present, and during reoxidation 30%. With NADH reduction there is little difference between the pattern of disappearance of the low-spin ferric heme signals in the absence or presence of cytochrome c. The copper and high-spin heme signals, however, disappear at higher titrant concentrations in the presence of cytochrome c than in its absence. In these titrations, as well as in those with ferrocytochrome c, the quantitative balance indicates that, in addition to EPR-detectable components, EPR-undetectable components are also reduced, increasingly so at higher titrant concentrations. The quantity of EPR-undectable components reduced appears to be inverely related to pH. A similar inverse relationship exists between pH and appearance of high-spin signals during yhe titration. At pH 9.3 the quantity of heme represented in the high-spin signals is less than 5%, whereas it approximately doubles from pH 7.4 to pH 6.1. In the presence of CO less of the low-spin heme and copper signals disappears for the same quantity of titrant consumed, again implying reduction of EPR undetectable components. At least one of these components is represented in a broad absorption band centered at 655 nm. The stoichiometry observed on reoxidation, particularly in the presence of CO, is not compatible with the notion that the copper signal represents 100% of the active copper of the enzyme as a pair of interacting copper atoms.

Anaerobiosis↗
PubMed1986

Fluorometric titration of the sarcoplasmic reticulum adenosinetriphosphatase calcium sites in the presence of vanadate.

Titration of the specific calcium binding sites of sarcoplasmic reticulum ATPase was carried out by measurements of intrinsic fluorescence in the absence and in the presence of vanadate. The previous finding that vanadate binding to the enzyme inhibits high-affinity calcium binding was confirmed. In addition, taking advantage of the slow kinetics of vanadate association and dissociation from the enzyme, we were able to titrate the fraction of sites remaining in the high affinity state in the presence of non-saturating vanadate. These sites were demonstrated to retain the characteristics displayed by the high-affinity sites in the absence of vanadate, and yielded information consistent with a competitive inhibition between vanadate and calcium. Reversal of the vanadate effect and reconversion of the binding sites to the high-affinity state was demonstrated by adding appropriate calcium concentrations to the enzyme-vanadate complex, and showing the appearance of the intrinsic fluorescence signal which is indicative of calcium occupancy of the sites in the high-affinity state. Partial or total reversal of the vanadate effect was obtained with very slow kinetics following addition of micromolar calcium or, at a somewhat faster rate, following addition of millimolar calcium. The latter experiments yielded titration of the binding sites in the low-affinity state, with a dissociation constant of approx. 2 mM at neutral pH and 10 mM Mg2+. The time course of the fluorescence rise following addition of calcium in the presence of vanadate was more rapid in 'leaky' than in native sarcoplasmic reticulum vesicles, suggesting an intravesicular orientation of the low-affinity calcium sites involved in the reversal of the vanadate effect. Our observations provide experimental support for the postulated mechanism of high- and low-affinity interconversion of the ATPase calcium binding sites, and its dependence on the occupancy of the phosphorylation site by vanadate.

Adenosine Triphosphatases↗
PubMed1977

Resolution of independently titrating spectral components in the ultraviolet circular dichroism of subtilisin enzymes by matrix rank analysis.

The ultraviolet circular dichroism of di-isopropylphophoryl-subtilisins Carlsberg and Novo (EC 3.4.21.14) has been examined as a function of pH. The CD of these enzymes below 260 nm is invariant over the pH interval 4 to 12, below or above which spectral changes occur suggesting a transition to a random coil form. Above pH 8 contributions due to the ionization of tyrosyl residues appear in the CD above 260 nm as bands shifted to longer wavelengths. Three independently titratable components, obtained by matrix rank analysis, account for the observed CD spectral changes above 260 nm of Dip-subtilisin Carlsberg in the pH interval 8 to 12. By contrast, two components were derived for the Novo enzyme. The identities of the matrix rank components were surmised from their apparent pKa values. One component of both subtilisin enzymes corresponds to the CD of the "buried" or irreversibly titratable tyrosyl residues of the enzyme. The other matrix rank components correspond to the CD of the "exposed" or freely ionizable tyrosyl residues. These residues are optically active only in the ionized state. Two types of "exposed" tyrosyl residues, arising because of differing sensitivity to the ionization of the "partially buried" or abnormally titrating tyrosyl residues, are evident in Dip-subtilisin Carlsberg. A pH-induced local conformational change in this enzyme is proposed to account for this behavior. The "partially buried" tyrosyl residues of both subtilisins appear to be devoid of optical activity in either the tyrosyl or tyrosylate form.

Circular Dichroism↗
PubMed1975

Hydrogen-ion titration curve of ovomucoid.

A systematic study of the H+ titration curve of purified ovomucoid was made at three temperatures (15, 25 and 35 degrees C) and three ionic strengths (0.05, 0.15 and 1.0). In all, 49 protons were dissociated reversibly in the pH range, 2.0-12.0. From the analysis of the results up to pH 12.0, the numbers of different dissociable groups per 28 300 g protein, together with their intrinsic pK values in parentheses were found tp be' 27 sode-chain carboxyl (pKint=4.0), four imidazole (pKint=6.5), one alpha-amino (pKint=7.5), 12 epsilon-amino (pKint=9.6), one guanidino (pKint=11.8) and one alpha-carboxyl group with abnormally low pK. The total number of basic nitrogens per mole of the protein was 22 so that four guanidino groups remained untitrated up to pH 12.0. Spectrophotometric titration showed that three out of five phenolic groups were titrated reversibly up to pH 11.9 with an intrinsic pK of 10.25; the remaining two groups became accessible only on protein denaturation. Viscosity results suggested absence of conformational change in the pH range 2.0-11.2. This explains the constancy of the pK values of carboxyl groups in the pH range 2.0-5.0. The empirical value of the electrostatic interaction factor, w, was 0.04, both in the carboxyl and phenolic regions.

Amino Acids↗
PubMed1978

pH titration study of cytochrome c peroxidase and apocytochrome c peroxidase.

A pH titration study of cytochrome c peroxidase and apocytochrome c peroxidase was carried out at 25 degrees C and 0.1 M ionic strength. The net charge on cytochrome c peroxidase due to proton association and dissociation varies from +32 at pH 2 to --50.2 at pH 12, while that of apocytochrome c peroxidase varies between +24.5 at pH 3 to --48 at pH 12. The apoprotein tented to aggregate below pH 3. Between pH 4 and 8, the titration behavior of both the native enzyme and the apoenzyme are consistent with the semi-empirical Linderstrøm-Lang theory. Between pH 9 and 12, the titration behavior of both the holo- and apoproteins suggest they assume a more extended conformation which reduces the electrostatic interaction charged groups on the surface. In the acid region, between pH 4 and 3, a similar transition occurs in which the protein expands 40% based on the electrostatic factor of the Linderstrøm-Lang theory.

Apoenzymes↗
PubMed1981

Neuronotrophic factors and their antibodies: in vitro microassays for titration and screening.

Using nerve growth factor (NGF), anti-NGF sera and dissociated neonatal mouse dorsal root ganglionic neurons we present a microculture assay methodology for (1) the titration of neurotrophic factor (NTF) activity in monolayer culture, (2) the titration of NTF antibodies which 'block' NTF biological activity, (3) the titration of NTF antibodies that bind and remove (sequester) NTF from culture medium and (4) a large-scale, convenient, and rapid screening for NTF biological activity as well as for NTF 'blocking' or 'sequestering' antibodies. These quantitative and qualitative in vitro microimmunoassays should be applicable to any neuronotrophic factor or its antibody, even when the agent is only available in crude, unpurified form. Since the microculture systems permit the simultaneous screening of one thousand samples per day they should be useful for the detection and quantitation of monoclonal antibodies present in hybridoma-conditioned media.

Animals↗
PubMed1988

Molecular titration as a means of calibrating enzyme reference materials.

Active site titration provides a means of calibrating enzyme reference materials in molecular concentration units independent from the incubation conditions used in kinetic assays. Such reference materials may serve as primary standards for calibrating any kinetic assay using the same active site. Active site titration of aspartate aminotransferase has been done by fluorimetric measurement of the half-cycle transamination of the phosphopyridoxal form. Another promising approach is the stoichiometric titration with specific suicide substrates such as vinylglycine. Expression of results in molecular concentration units requires that both the primary enzyme standard and the enzyme as measured in blood plasma show similar turnover numbers and substrate specificity in the kinetic assay being used. This is best achieved with purified reference materials of human origin. If the assay in plasma measures the sum of several isoenzymes having different turnover numbers, then the calibration is no longer absolute but becomes method-dependent.

Binding Sites↗
PubMed1996

A method for titration of inhibiting antibodies to bacterial immunoglobulin A1 proteases in human serum and secretions.

Bacterial IgA1 proteases specifically cleave IgA1, including S-IgA1, molecules into Fab alpha and Fc alpha fragments. Hereby these enzymes interfere with the protective functions of antibodies belonging to this isotype. Antibodies inhibiting IgA1 proteases have been detected in humans, but the titration of such antibodies is a matter of methodological concern. Because human serum and secretions contain IgA1 substrate, it is impossible to provide uniform substrate conditions for samples of IgA1 protease incubated with inhibitors differing in their origin and state of dilution. This study demonstrates that such variations in substrate are not prohibitive for a reliable titration of inhibiting antibodies. This was evident from experiments demonstrating that the variations do not interfere with the quantification of residual IgA1 protease activity provided the activity is measured in terms of the proportion of IgA1 substrate cleaved during incubation. Proportions of cleaved IgA1 were measured by exploiting the differential reactivity of cleaved and intact IgA1 molecules in an ELISA using anti-Fc alpha and enzyme-conjugated anti-light chain antibodies for catching and development, respectively. A protocol for the titration of IgA1 protease-inhibiting antibodies based on this ELISA is described. By application of the protocol to chromatographic fractions of saliva, IgA1 protease-inhibiting activity was found to co-purify with salivary S-IgA.

Adult↗
PubMed1980

Titration procedure with rats using a nose poke response and tail shock.

An operant titration procedure that provides relatively stable within-session shock thresholds (0.15--0.25 mA) within a week of training is described. Rats are placed into Plexiglas restraint tubes having a hole at one end through which the animal can poke its nose to break a photobeam; when the photobeam is broken, a response is counted. The tail of the animal is firmly held by a Plexiglas plug and an electrode connected to a programmable titration shocker is attached to the tail. Conditioned nose poke response are made after about 15 min during the first 30 min session. The titration procedure was found to be sensitive to the analgesic effect of morphine. Significant increases in the median shock level tolerated was observed after 3 mg/kg, while response rate was not altered. Dose-related increases in threshold after 6 and 9 mg/kg of morphine were associated with decreases in the rate of nose poking. The technique offers several advantages in the study of chemical induced alterations in pain or reactivity, including rapidity of initial training, relatively short time to establish median shock thresholds, minimum involvement of motor components in the response, and sensitivity to a psychopharmacological tool.

Animals↗
PubMed1980

An improved apparatus for intragastric titration in the conscious dog.

An apparatus for automatic intragastric titration with on-line display of results has been described. The apparatus has been validated by titration of exogenous acid injected into the test meal in a reservoir and in vivo by assessing the secretory response of a dog with a gastric fistula to a test meal. A titration display unit provides a record of the secretory response both as a digital printout and a bar chart display. Cimetidine (2 mg kg-1h-1) significantly reduced the secretory response to a test meal.

Animals↗
PubMed1980

Isoelectric focusing following by electrophoresis of proteins for visualizing their titration curves by zymogram and immunofixation.

After isoelectric focusing followed by electrophoresis at right angles in the same gel slab, it is possible to visualize the titration curve of proteins by zymograms or immunofixation even of an unpurified sample. This information can be very useful for the selection of the proper purification strategy by charge-dependent methods, e.g. ion-exchange chromatography, zone and disc electrophoresis and isotachophoresis. The titration curve also gives information on the stability of the protein as a function of the prevailing pH of the medium, in the pH 3-10 range. A region of instability is found for most proteins in acidic conditions, below pH 4.5, while most proteins are stable in the alkaline pH region, at least up to pH 10. The best method for developing zymograms and immunoprints appears to pH 10. The best method for developing zymograms and immunoprints appears to be the 'sandwich technique', by which a thin agarose slab, cast on an hydrophilic polyester sheet, and impregnated with appropriate reagents, is left in contact with a polyacrylamide gel thin layer used to generate the titration curves.

Alcohol Oxidoreductases↗