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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The (low loaded) biological nutrient removing activated sludge process is the generally accepted and applied municipal wastewater treatment method in the Netherlands. The hydraulical and biological flexibility, robustness and cost efficiency of the process for advanced removal of nutrients like nitrogen and phosphorus without (too much) chemicals results in a wide application of the activated sludge process within Dutch waterboards. Presumably, wastewater treatment plants will have to contribute to the improvement of the quality of the receiving surface waters by producing cleaner effluent. In this perspective, the Dutch research organisation STOWA initiated a research project entitled "The Boundaries of the Activated Sludge Process" to investigate the possibilities and limitations of activated sludge processes to improve the effluent quality. It is concluded that the activated sludge process as applied and operated at WWTP's in the Netherlands has the potential to perform even better than the current effluent discharge standards (10 mg Ntotal/l and 1 mg Ptotal/l). Reaching the B-quality effluent (<5mg Ntotal/l and <0.3 mg Ptotal/l) will be possible at almost all WWTPs without major adjustments under the conditions that: the sludge load is below 0.06 kg BOD/kg TSS.d the internal recirculation is above 20 the BOD/N ratio of the influent is above 3. Complying with the A-quality effluent (<2.2 Ntotal/l and <0.15 mg Ptotal/l) seems to be difficult (but not impossible) and requires more attention and insight into the activated sludge process. Optimisation measures to reach the A-quality effluent are more thorough and are mostly only achievable by additional construction works (addition of activated sludge volume, increasing recirculation capacity, etc.). It is furthermore concluded that the static HSA-results are comparable to the dynamic ASM-results. So, for fast determinations of the limits of technology of different activated sludge processes static modelling seems to by sufficient.
Water Sci Technol 2008
PMID:The limits and ultimate possibilities of technology of the activated sludge process. 1900 24

Abstract Effect of atrial natriuretic peptide (ANP) on the vasopressin response to osmotic stimulation (Experiment I) as well as to hemorrhage (Experiment II) was investigated in anesthetized dogs. Moreover, cardiovascular function and renal water and electrolyte excretion were studied. In Experiment I, 2.5 M NaCI, containing 0.02 mug.kg (1) of ANP, was infused intravenously at a rate of 0.2 ml.kg(-1), min (1) after one bolus injection of 0.75 mug.kg (1) ANP (HSA group). In the control group, 2.5 M NaCI alone (HS group) was infused. The infusion was continued for 75 min. In Experiment II, 0.15 M NaCI, containing the identical dose of ANP to Experiment I (HA group), or 0.15 M NaCI alone (H group) was infused intravenously during bleeding at a rate of 1 ml.kg(-1).min (-1) for 40 min. In Experiment I, infused ANP suppressed the vasopressin response to a mild osmotic stimulation, but not to a strong osmotic stimulation and attenuated ANP release and a rise in arterial and central venous pressures in response to plasma volume expansion, without the enhanced natriuresis. In Experiment II, infused ANP neither impaired the vasopressin response to bleeding nor potentiated a fall in mean arterial pressure and central venous pressure. In conclusion, ANP at physiological and/or supraphysiological range may suppress the vasopressin response to a mild osmotic stimulation, but not to a strong osmotic stimulation and to hemorrhage. In addition, ANP given intravenously may attenuate ANP release and a rise in blood pressure without any natriuresis.
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PMID:Effect of atrial natriuretic Peptide on the vasopressin response to osmotic and hemorrhagic stimuli in dogs. 1921 36

Gold nanoparticles the size of about 10 nm were prepared by improved trisodium citrate reduction procedure, and were used to label goat anti-human IgG to obtain a sensitive spectral probe for IgG in the condition of pH 6.5. The immune reaction of nanogold-labeled IgG antibody (anti-IgG) with the antigen IgG took place to form the nanogold immune complex in pH 7.O Na2HPO4-C6H8O7 buffer solution and in the presence of polyethylene (PEG). The optimal immunoreaction conditions were pH 7.0, 10.76 microg x mL(-1) nanogold-labeled anti-IgG, 8.0% PEG 6000 and incubation time of 30 min under the ultrasonic irradiation. After centrifuging for 15 min at 16000 rpm, the excess nanogold-labeled anti-IgG in the upper solutions was obtained, and was used to catalyze the colored particle reaction of HAuCl4 with NH2 OH x HCl to produce gold particles with bigger size. The influence of pH value, HAuCl4 and NH2OH x HCl concentration, and reaction temperature and time on the immunonanogold catalytic reaction was considered spectrophotometrically. A pH 2.27 Na3C6H5O7-HCl buffer solution, 0.094 mmol x L HAuCl4, 1.92 mmol x L NH22OH x HCl, and reaction time of 6 min at 30 degrees C water bath were chosen for use. Results demonstrated that with increasing IgG, the concentration of gold labeled anti-IgG in the upper solution decreased, and the absorbance decreased linearly. Linear relationships between the decreased absorbance at 700 nm and the IgG concentration CIgG in the range of 0.10-10 ng x mL(-1) were obtained. Its regress equation was deltaA(760 nm) = 0.0144c(IgG) + 0.0042, the related coefficient was 0.9926, and the detection limit reached 0.06 ng x mL(-1) IgG. The influence of foreign substances on the determination of 3 ng x mL(-1) IgG was examined, with the relative error +/-10%. Results showed that the following coexistent substances had no impact on the assay: 6000 ng x mL(-1) HSA, 6000 ng x mL(-1) gluocose, 6000 ng x ml(-1) Zn(II), 3000 ng x mL(-1) IgA, 3000 ng x mL(-1) Ca(II), 3000 ng x mL(-1) L-arginine, 3000 ng x mL(-1) beta-phenylalanine, 2400 ng x mL(-1) Cu(II), 2400 ng x mL(-1) EDTA, 2400 ng x mL(-1) L-cystinol etc. This showed that the assay has high selectivity. The sensitive, rapid and highly specific assay was applied to the quantification of IgG in human sera, with satisfactory results.
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PMID:[Immunonanogold catalytic spectrophotometric determination of trace IgG]. 1924 17

The fluorescence photobleaching recovery method with pulse-position modulation (PPM) of bleaching/probing irradiation is presented. This approach is modification of previously announced photobleaching recovery under decaying photobleaching (FRDP) approach, which employs the amplitude control of irradiation intensity. Underlying idea was to solve the problem of setup nonlinearity by methodical modification that was successfully done. The irradiation intensity is series of equal bleach-probe pulses with increasing distance. The more sophisticated series was proposed as a convolution of subseries, which one characterizing its own time scale. It allows to detect the fluorescence kinetics in the wide range of time and of different nature simultaneously. The method was applied on model systems as FITC-HSA in the water/glycerol mixture and FITC-DMPE in the POPC multibilayers. The method allowed to detect and investigate diffusion processes, presence immobile fraction, effect of limited area of liposomes and reversible fluorescence kinetics.
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PMID:Fluorescence photobleaching recovery method with pulse-position modulation of bleaching/probing irradiation. 1935 44

In the pH 7.2 Na2HPO4-NaH2PO4 buffer solutions and in the presence of PEG-6000, fenvalerate (Fen) antisera was combined with Fen specifically, and aggregated to form immune complex particles that exhibited five resonance scattering peaks at 350, 390, 420, 440 and 480 nm respectively. The peak at 390 nm was the strongest and was chosen for use. Fen concentration (c) in the range of 0.20 to 6.40 microg x mL(-1) was proportional to the resonance scattering intensity at 390 nm. Its regression equation was DeltaIRS 23.05c-1.39, the correlation coefficient was 0.9978, and the detection limit was 0.07 microg x mL(-1). Effects of buffer solution type, pH value, buffer solution volume, fenvalerate antisera concentration, PEG-6000 concentration, incubation temperature and time on the resonance scattering intensity were considered in detail. With pH (5.8-8.0) increasing, the IRS and Ib all decreased. When the pH value was at 7.2, the DeltaIRS was bigger. Three buffer solutions of pH 7.2, including Na2HPO4-citric acid, Na2HPO4-KH2PO4 and Na2HPO4-NaH2PO4, were examined. The pH 7.2 Na2HPO4-NaH2PO4 buffer solution gives the biggest DeltaIRS value. PEG-6000 could enhance the DeltaIRS value. When the concentration of PEG-6000 was 50.0 mg x mL(-1), the DeltaIRS was achieved at max. Fen was a stable chemical. The IRS increased within 20 min,while the DeltaIRS remained constant when incubation time was in the range of 20-40 min. The condition of a pH 7.2 Na2HPO4-NaH2PO4 buffer solution-50.0 mg x mL(-1) PEG-6000-6.67 microg x mL(-1) Fen antisera-30 degrees C-incubation time 20 min was chosen. According to the procedure, the influence of foreign substances on the determination of 1.60 microg x mL(-1) Fen was examined, within a relative error of +/- 5%. Results showed that the following coexistent substances had no impact on the RS assay: 96 microg x mL(-1) ametryne, 96 microg x mL(-1) m-aminotoluene, 48 microg x mL(-1) simetryne, 48 microg x mL(-1) p-aminotoluene,80 microg x mL(-1) BSA, 80 microg x mL(-1) HSA, 80 microg x mL(-1) Fe3+, 80 microg x mL(-1) Mg2+, 160 microg x mL(-1) Ca2+, and 160 microg x mL(-1) glucose. The results indicated that this RSS assay has good selectivity. This immune resonance scattering spectral assay was applied to the determination of Fen in waste water samples with satisfactory results. The recovery was in the range of 92.91%-101.25%, and the relative standard deviation was in the range of 1.71%-4.80%.
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PMID:[Immune resonance scattering spectral analysis of fenvalerate]. 1938 42

Ferric human serum heme-albumin (heme-HSA) shows a peculiar nuclear magnetic relaxation dispersion (NMRD) behavior that allows to investigate structural and functional properties. Here, we report a thermodynamic analysis of NMRD profiles of heme-HSA between 20 and 60 degrees C to characterize its hydration. NMRD profiles, all showing two Lorentzian dispersions at 0.3 and 60 MHz, were analyzed in terms of modulation of the zero field splitting tensor for the S=5/2 manifold. Values of correlation times for tensor fluctuation (tau(v)) and chemical exchange of water molecules (tau(M)) show the expected temperature dependence, with activation enthalpies of -1.94 and -2.46+/-0.2 kJ mol(-1), respectively. The cluster of water molecules located in the close proximity of the heme is progressively reduced in size by increasing the temperature, with DeltaH=68+/-28 kJ mol(-1) and DeltaS=200+/-80 J mol(-1) K(-1). These results highlight the role of the water solvent in heme-HSA structure-function relationships.
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PMID:Thermodynamic analysis of hydration in human serum heme-albumin. 1946 61

The development of nanosystems applied to rapid and sensitive measurement of biomarkers in fluid samples is a current major goal in diagnostic biomedicine. In this article, we report the accurate and reliable detection of anti-HSA (human serum albumin) antibodies by protein-functionalized magnetic nanospherical probes due to the reversible alteration of their microaggregation state induced by protein antibody-specific interaction, sensed as changes in the T(2) relaxation time of surrounding water molecules. Once the optimal parameters were adjusted, the method proved to be very sensitive, providing concentration- and time-dependent responses. Furthermore, we demonstrate that the developed immunoassay is able to quantitatively determine the biomarker concentration from T(2) linear correlation, thereby supplying a rapid, yet accurate, assay with sensitivity in the femtomolar range. The high susceptibility and stability of these magnetic nanoparticles, as well as their accessible synthetic preparation, make these nanosensors a promising new tool for versatile and effective medical diagnostics.
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PMID:Femtomolar detection of autoantibodies by magnetic relaxation nanosensors. 1948 Oct 52

Elevated tumor interstitial fluid pressure (TIFP) is a characteristic of most solid tumors. Clinically, TIFP may hamper the uptake of chemotherapeutic drugs into the tumor tissue reducing their therapeutic efficacy. In this study, a means of modulating TIFP to increase the flux of macromolecules into tumor tissue is presented, which is based on the rationale that elevated plasma colloid osmotic pressure (COP) pulls water from tumor interstitium lowering the TIFP. Concentrated human serum albumin (20% HSA), used as an agent to enhance COP, reduced the TIFP time-dependently from 8 to 2 mm Hg in human tumor xenograft models bearing A431 epidermoid vulva carcinomas. To evaluate whether this reduction facilitates the uptake of macromolecules, the intratumoral distribution of fluorescently conjugated dextrans (2.5 mg/ml) and cetuximab (2.0 mg/ml) was probed using novel time domain nearinfrared fluorescence imaging. This method permitted discrimination and semiquantification of tumor-accumulated conjugate from background and unspecific probe fluorescence. The coadministration of 20% HSA together with either dextrans or cetuximab was found to lower the TIFP significantly and increase the concentration of the substances within the tumor tissue in comparison to control tumors. Furthermore, combined administration of 20% HSA plus cetuximab reduced the tumor growth significantly in comparison to standard cetuximab treatment. These data demonstrate that increased COP lowers the TIFP within hours and increases the uptake of therapeutic macromolecules into the tumor interstitium leading to reduced tumor growth. This model represents a novel approach to facilitate the delivery of therapeutics into tumor tissue, particularly monoclonal antibodies.
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PMID:Increased plasma colloid osmotic pressure facilitates the uptake of therapeutic macromolecules in a xenograft tumor model. 1964 11

We report on the rotational reorientation dynamics associated with loop 1 of domain I within a large multidomain protein (human serum albumin, HSA) when it is dissolved in binary mixtures of ionic liquid (1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide ([C4mim][Tf2N]), 1-butyl-3-methylimidazolium tetrafluoroborate ([C4mim][BF4]), or 1-butyl-3-methylimidazolium hexafluorophosphate ([C4mim][PF6])) and distilled deionized water (ddH2O) as a function of temperature and water loading. In IL/2% ddH2O (v/v) mixtures, loop 1 of domain I is more significantly denatured in comparison to the protein dissolved in aqueous solutions containing strong chemical denaturants (e.g., 8 M guanidine HCl (Gu.HCl) or urea). As water loading increases, there is evidence for progressive refolding of loop 1 of domain I followed by recoupling with domains I, II, and III in the [C4mim][BF4]/ddH2O mixtures at 20 degrees C. Above 30% (v/v) water, where domain I appears refolded, the Ac reporter molecule's semiangle steadily decreases from 35 degrees to 20 degrees with increasing water loading. From the perspective of domain I in HSA, this behavior is similar to the effects of dilution from 4 to 0 M Gu.HCl in aqueous solution. Overall, these results lend insight into the tangle of biocatalytic and structural/dynamical mechanisms that enzymes may undergo in ionic liquid-based systems. It will be particularly motivating to extend this work to include enzyme-attuned ionic liquids shown to improve biocatalytic performance beyond that possible in the native (predominantly aqueous) setting.
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PMID:Dynamics of loop 1 of domain I in human serum albumin when dissolved in ionic liquids. 1971 30

The standard solution-depletion method is implemented with SDS-gel electrophoresis as a multiplexing, separation-and-quantification tool to measure competition between two proteins (i and j) for adsorption to the same hydrophobic adsorbent particles (either octyl sepharose or silanized glass) immersed in binary-protein solutions. Adsorption kinetics reveals an unanticipated slow protein-size-dependent competition that controls steady-state adsorption selectivity. Two sequential pseudo-steady-state adsorption regimes (State 1 and State 2) are frequently observed depending on i, j solution concentrations. State 1 and State 2 are connected by a smooth transition, giving rise to sigmoidally-shaped adsorption-kinetic profiles with a downward inflection near 60 min of solution/adsorbent contact. Mass ratio of adsorbed i, j proteins (m(i)/m(j)) remains nearly constant between States 1 and 2, even though both m(i) and m(j) decrease in the transition between states. State 2 is shown to be stable for 24 h of continuous-adsorbent contact with stagnant solution whereas State 2 is eliminated by continuous mixing of adsorbent with solution. In sharp contrast to binary-competition results, adsorption to hydrophobic adsorbent particles from single-protein solutions (pure i or j) exhibits no detectable kinetics within the timeframe of experiment from either stagnant or continuously mixed solution, quickly achieving a single steady-state value in proportion to solution concentration. Comparison of binary competition between dissimilarly-sized protein pairs chosen to span a broad molecular-weight (MW) range demonstrates that selectivity between i and j scales with MW ratio that is proportional to protein-volume ratio (ubiquitin, Ub, MW=10.7 kDa; human serum albumin, HSA, MW=66.3 kDa; prothrombin, FII, 72 kDa; immunoglobulin G, IgG, MW=160 kDa; fibrinogen, Fib, MW=341 kDa). Results are interpreted in terms of a kinetic model of adsorption that has protein molecules rapidly diffusing into an inflating interphase that is spontaneously formed by bringing a protein solution into contact with a physical surface (State 1). State 2 follows by rearrangement of proteins within this interphase to achieve the maximum interphase concentration (dictated by energetics of interphase dehydration) within the thinnest (lowest volume) interphase possible by ejection of interphase water and initially-adsorbed proteins. Implications for understanding biocompatibility are discussed using a computational example relevant to the problem of blood-plasma coagulation.
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PMID:Volumetric interpretation of protein adsorption: kinetics of protein-adsorption competition from binary solution. 1975 50


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