http://www.bibsonomy.org/burst/user/biblio24/methodologyBibSonomy BuRST Feed for /user/biblio24/methodology2008-08-21T13:03:52+02:00http://www.bibsonomy.org/bibtex/2a3b4759cb002a502b7fcd032c29ab19c/biblio24biblio242006-07-07T01:10:50+02:00antibody methodology statistic spr analysis review affinity <span style="color:#555555;">M. H. <a href="http://www.bibsonomy.org/author/Van Regenmortel">Van Regenmortel</a> and D. <a href="http://www.bibsonomy.org/author/Altschuh">Altschuh</a> and J. <a href="http://www.bibsonomy.org/author/Chatellier">Chatellier</a> and L. <a href="http://www.bibsonomy.org/author/Christensen">Christensen</a> and N. <a href="http://www.bibsonomy.org/author/Rauffer-Bruyère">Rauffer-Bruy&#232;re</a> and P. <a href="http://www.bibsonomy.org/author/Richalet-Secordel">Richalet-Secordel</a> and J. <a href="http://www.bibsonomy.org/author/Witz">Witz</a> and G. <a href="http://www.bibsonomy.org/author/Zeder-Lutz">Zeder-Lutz</a> </span><em>J Mol Recognit</em><em>11(1-6):163--167</em>(<em>1998</em>)Fri Jul 07 01:10:50 CEST 2006IBMC, Strasbourg, France.J Mol Recognit1-6163--167Measurement of antigen-antibody interactions with biosensors.111998antibody methodology statistic spr analysis review affinity The introduction in 1990 of a new biosensor technology based on surface plasmon resonance has revolutionized the measurement of antigen-antibody binding interactions. In this technique, one of the interacting partners is immobilized on a sensor chip and the binding of the other is followed by the increase in refractive index caused by the mass of bound species. The following immunochemical applications of this new technology will be described: (1) functional mapping of epitopes and paratopes by mutagenesis; (2) analysis of the thermodynamic parameters of the interaction; (3) measurement of the concentration of biologically active molecules; (4) selection of diagnostic probes.http://www.bibsonomy.org/bibtex/2707c5aebeba697dc4c64731bf2795c4c/biblio24biblio242006-07-07T01:10:50+02:00epitope mapping spr methodology <span style="color:#555555;">B. <a href="http://www.bibsonomy.org/author/Johne">Johne</a> and M. <a href="http://www.bibsonomy.org/author/Gadnell">Gadnell</a> and K. <a href="http://www.bibsonomy.org/author/Hansen">Hansen</a> </span><em>J Immunol Methods</em><em>160(2):191--198</em><em>April1993. </em>Fri Jul 07 01:10:50 CEST 2006Diagnostica R \& D, Nycomed Pharma AS, Oslo, Norway.J Immunol MethodsApril2191--198Epitope mapping and binding kinetics of monoclonal antibodies studied by real time biospecific interaction analysis using surface plasmon resonance.1601993epitope mapping spr methodology The interaction between human heart myoglobin and ten specific monoclonal antibodies was investigated with a new biosensor technology, real time biospecific interaction analysis (RT BIA), using surface plasmon resonance. Analysis of association and dissociation kinetics was monitored in real time, with unlabelled reactants. Antibody isotyping was rapid and simple. Epitope mapping with RT BIA confirmed, with substantial time saving, the sum of results obtained in conventional labelled systems. Monoclonal antibodies with four different epitope specificities and optimal binding function were selected for a myoglobin sandwich assay with enhanced sensitivity. BIAcore can be used directly as a diagnostic tool, or as an analytical tool in immunoassay development.http://www.bibsonomy.org/bibtex/2a30aca522996ede82f1c0509827e6c06/biblio24biblio242006-07-07T01:10:50+02:00antibody immunoassay methodology <span style="color:#555555;">B. <a href="http://www.bibsonomy.org/author/Hock">Hock</a> and M. <a href="http://www.bibsonomy.org/author/Rahman">Rahman</a> and S. <a href="http://www.bibsonomy.org/author/Rauchalles">Rauchalles</a> and A. <a href="http://www.bibsonomy.org/author/Dankwardt">Dankwardt</a> and M. <a href="http://www.bibsonomy.org/author/Seifert">Seifert</a> and S. <a href="http://www.bibsonomy.org/author/Haindl">Haindl</a> and K. <a href="http://www.bibsonomy.org/author/Kramer">Kramer</a> </span><em>Journal of Molecular Catalysis B: Enzymatic</em><em>7(1-4):115--124</em><em>September1999. </em>Fri Jul 07 01:10:50 CEST 2006Journal of Molecular Catalysis B: EnzymaticSeptember1-4115--124Stabilisation of immunoassays and receptor assays71999antibody immunoassay methodology Stability of immunoassays and receptor assays depends on the integrity of antibodies and receptors as binding proteins for the analytes. In addition, coating conjugates, tracers, and if applicable, enzyme substrates have to be considered. In this study, temperature effects on monoclonal and recombinant antibodies for atrazine and on estrogen receptors were investigated in the presence and absence of stabilisers. Monoclonal antibodies for atrazine suffered only moderate activity losses after a 10-day incubation at 37[deg]C which could be demonstrated by shifts of the calibration curves. Even more remarkable was the resistance of the analogous recombinant Fab fragments to temperatures up to 50[deg]C. However, the estrogen receptor showed severe losses already after a 3-day exposure at 4[deg]C. Various stabilisers were tested. In the case of antibodies, several commercial stabilisers prevented activity losses at higher temperatures. Improved stabilisation strategies are discussed. They are mainly seen in the selection of temperature-resistant recombinant antibodies and in the reduction of assay components.http://www.bibsonomy.org/bibtex/2081b02b688bd100c86230e0d47363a43/biblio24biblio242006-07-07T01:10:50+02:00biosensor methodology <span style="color:#555555;">K. A. <a href="http://www.bibsonomy.org/author/Giuliano">Giuliano</a> and D. L. <a href="http://www.bibsonomy.org/author/Taylor">Taylor</a> </span><em>Trends Biotechnol</em><em>16(3):135--140</em><em>March1998. </em>Fri Jul 07 01:10:50 CEST 2006Cellomics Inc., Pittsburgh, PA 15238, USA.Trends BiotechnolMarch3135--140Fluorescent-protein biosensors: new tools for drug discovery.161998biosensor methodology Recent improvements in target discovery and high-throughput screening have increased the pressure at key points along the drug-discovery pipeline. High-content screening was developed to ease the bottlenecks formed at the target-validation and lead-optimization points, and a new generation of reagents that report on specific molecular processes in living cells (fluorescent-protein biosensors) have been important in its development. Creative designs of fluorescent-protein biosensors have emerged and been used to measure the molecular dynamics of macromolecules, metabolites and ions. Recent applications of fluorescent-protein biosensors to biological problems have provided a foundation for their use in biotechnology.http://www.bibsonomy.org/bibtex/26f20515c77d9e96a81cf958a5681c43e/biblio24biblio242006-07-07T01:10:50+02:00methodology electrochemistry review <span style="color:#555555;">Ivan <a href="http://www.bibsonomy.org/author/Švancara">&#352;vancara</a> and Karel <a href="http://www.bibsonomy.org/author/Vytřas">Vyt&#345;as</a> and Ji&#345;&#237; <a href="http://www.bibsonomy.org/author/Barek">Barek</a> and Ji&#345;&#237; <a href="http://www.bibsonomy.org/author/Zima">Zima</a> </span><em>Critical Reviews in Analytical Chemistry</em><em>31(4):311--345</em><em>October2001. </em>Fri Jul 07 01:10:50 CEST 2006Department of Analytical Chemistry, Faculty of Chemical Technology, University of Pardubice, nam. Cs. legii 565, CZ-532 10 Pardubice, Czech RepublicCritical Reviews in Analytical ChemistryOctober4311--345Carbon Paste Electrodes in Modern Electroanalysis312001methodology electrochemistry review Recent trends and advances in the electrochemistry with both unmodified and modified carbon paste electrodes are reviewed (247 refs.). Present day knowledge of their basic physico-chemical properties and characteristics is surveyed, including some specifics important in electrochemical measurements. Special attention is paid to the possibilities of carbon paste-based electrodes in electrochemical investigations and in modern electroanalysis of inorganic ions or molecules, organic substances, biologically important compounds, and pharmaceuticals.http://www.bibsonomy.org/bibtex/28342c961c983eeea16234a26b5530ff8/biblio24biblio242006-07-07T01:10:50+02:00methodology biosensor amperometry electrochemistry <span style="color:#555555;">H. <a href="http://www.bibsonomy.org/author/Durliat">Durliat</a> and C. <a href="http://www.bibsonomy.org/author/Causserand">Causserand</a> and M. <a href="http://www.bibsonomy.org/author/Comtat">Comtat</a> </span><em>Analytica Chimica Acta</em>(<em>1990</em>)Fri Jul 07 01:10:50 CEST 2006Analytica Chimica Acta309--311Bienzyme amperometric lactate-specific electrode2311990methodology biosensor amperometry electrochemistry The electrode, based on a lactate dehydrogenase and a diaphorase, permits the assay of -lactate in the concentration range 0.2-8 mM with a response time of about 40 s. Both the enzymes are commercially available. The amperometric detection of hexacyanoferrate(II) at a platinum electrode is done at 0.3 V (vs. SCE) instead of 0.8 V as in the detection of NADH, improving the selectivity of the sensor.http://www.bibsonomy.org/bibtex/2b136b4b30fb6b6992620830b10eca4c0/biblio24biblio242006-07-07T01:10:50+02:00methodology electrochemistry biosensor theory <span style="color:#555555;">N. <a href="http://www.bibsonomy.org/author/Fogh-Andersen">Fogh-Andersen</a> and P. D. <a href="http://www.bibsonomy.org/author/Wimberley">Wimberley</a> and J. <a href="http://www.bibsonomy.org/author/Thode">Thode</a> and O. <a href="http://www.bibsonomy.org/author/Siggaard-Andersen">Siggaard-Andersen</a> </span><em>Clin Chim Acta</em><em>189(1):33--38</em><em>July1990. </em>Fri Jul 07 01:10:50 CEST 2006Department of Clinical Chemistry, Herlev Hospital, Denmark.Clin Chim ActaJuly133--38Direct reading glucose electrodes detect the molality of glucose in plasma and whole blood.1891990methodology electrochemistry biosensor theory It is the activity that determines the direction of chemical processes, transport, etc. and thus provides the clinically more relevant information. Direct reading glucose electrodes consume glucose at a rate proportional to the glucose activity in the sample. The activity equals the molality (mmol glucose per kg water), so results from direct reading glucose electrodes must differ from the conventionally measured glucose concentration. This was observed in 159 whole blood samples which gave higher results from a direct reading glucose electrode than by our conventional method (y = 1.21x - 0.37 mmol/l). However, adjustment for the different water concentration due to salt, plasma proteins, and hemoglobin occupying space, gave results equal to the concentrations (y = 1.00x - 0.28 mmol/l, r = 0.997). Furthermore, results for samples with constant glucose concentration and varying albumin concentration correlated with the albumin concentration (r = 0.989), but not after adjustment for water concentration (r = 0.037, n.s.).http://www.bibsonomy.org/bibtex/2ccd0b7049ac3e0ee6b30f079840daafe/biblio24biblio242006-07-07T01:10:50+02:00methodology electrochemistry theory biosensor <span style="color:#555555;">N. <a href="http://www.bibsonomy.org/author/Fogh-Andersen">Fogh-Andersen</a> and P. <a href="http://www.bibsonomy.org/author/D&#039;Orazio">D'Orazio</a> </span><em>Clin Chem</em><em>44(3):655--659</em><em>March1998. </em>Fri Jul 07 01:10:50 CEST 2006Department of Clinical Biochemistry, Herlev Hospital, Denmark. nfa@post6.tele.dkClin ChemMarch3655--659Proposal for standardizing direct-reading biosensors for blood glucose.441998methodology electrochemistry theory biosensor Direct-reading glucose biosensors sense molality (glucose per unit water mass) in the sample. With aqueous calibration, a direct-reading glucose biosensor produces higher results in blood and plasma than methods measuring concentration, theoretically by the ratio of water concentrations in calibrator and sample. To confirm this, we measured glucose in 14- blood and 40 plasma samples with the direct-reading glucose sensor in the Chiron Model 860 Blood Gas and Critical Analyte System and with our routine method (ESAT 6660; Eppendorf). The Chiron instrument is calibrated with a 10 mmol/L (180 mg/dL0 glucose calibrator (mass concentration of water = 0.99 kg/L). Assuming normal water concentrations of 0.84 and 0.93 kg/L in blood and plasma, respectively, we multiplied results from the Chiron sensor by 0.84/0.99 and 0.93/0.99 to obtain concentrations in blood and plasma. This conversion resulted in agreement of results with our routine method. An individual conversion based on hematocrit in each whole-blood sample was less satisfactory. To avoid confusion over variously measured and reported glucose results and reference values, we suggest standardization and reporting of whole-blood glucose results as equivalent plasma concentrations. This proposal may be conveniently achieved by using a commercially available reference material for glucose, NIST SRM 965.http://www.bibsonomy.org/bibtex/2e4e4c126277126754b0df4d2cac9b461/biblio24biblio242006-07-07T01:10:50+02:00theory methodology biosensor electrochemistry <span style="color:#555555;">R. <a href="http://www.bibsonomy.org/author/Haeckel">Haeckel</a> and P. <a href="http://www.bibsonomy.org/author/Hänecke">H&#228;necke</a> </span><em>Clin Chem Lab Med</em><em>41(7):950--957</em><em>July2003. </em>Fri Jul 07 01:10:50 CEST 2006Institute for Laboratory Medicine, Zentralkrankenhaus Sankt-Juergen-Strasse, Bremen, Germany. rainer.haeckel@zkh-bremen-mitte.deClin Chem Lab MedJuly7950--957Problems of comparing blood glucose molality and molarity determined with an Omni, an EML 105 and an Ebio analyser.412003theory methodology biosensor electrochemistry The comparability between glucose concentrations measured in various sample systems is still a matter of debate. Decision limits are usually determined in venous plasma and then converted to either blood or to the aqueous compartment (activity). The conversion factors recommended have not yet been generally accepted. In the present study, glucose concentrations were determined in blood and plasma with an Ebio analyser (molarity) and in the aqueous compartment with both an EML 105 and an Omni (molality). All analytical results were referred to the same aqueous standard solution. The Ebio results agreed with reference method values in control materials. Concentrations determined in the various sample systems from patients (molarity) correlated well with the molality values measured either with the EML or the Omni. However, the mean values of the EML were not consistent with those derived theoretically by considering the different water content. With the Omni, only molality values in whole blood appeared plausible, but not in plasma, although the two sample systems should provide identical molality values. The EML results were almost identical in whole blood and plasma. Theoretically, glucose molality would be the ideal diagnostic quantity. However, no diagnostic advantage of molality determined in whole blood with the Omni vs. molarity values could be detected in a group of 40 non-diabetic and 27 diabetic subjects.http://www.bibsonomy.org/bibtex/2a5d3e6fce5459d77e5b5bc7240f7e695/biblio24biblio242006-07-07T01:10:50+02:00electrochemistry methodology biosensor theory <span style="color:#555555;">P. <a href="http://www.bibsonomy.org/author/D&#039;Orazio">D'Orazio</a> and R. W. <a href="http://www.bibsonomy.org/author/Burnett">Burnett</a> and N. <a href="http://www.bibsonomy.org/author/Fogh-Andersen">Fogh-Andersen</a> and E. <a href="http://www.bibsonomy.org/author/Jacobs">Jacobs</a> and K. <a href="http://www.bibsonomy.org/author/Kuwa">Kuwa</a> and W. R. <a href="http://www.bibsonomy.org/author/Külpmann">K&#252;lpmann</a> and L. <a href="http://www.bibsonomy.org/author/Larsson">Larsson</a> and A. <a href="http://www.bibsonomy.org/author/Lewenstam">Lewenstam</a> and A. H. <a href="http://www.bibsonomy.org/author/Maas">Maas</a> and G. <a href="http://www.bibsonomy.org/author/Mager">Mager</a> and J. W. <a href="http://www.bibsonomy.org/author/Naskalski">Naskalski</a> and A. O. <a href="http://www.bibsonomy.org/author/Okorodudu">Okorodudu</a> </span><em>Clin Chem</em><em>51(9):1573--1576</em><em>September2005. </em>Fri Jul 07 01:10:50 CEST 2006Instrumetation Laboratory, Lexington, MA, USA.Clin ChemSeptember91573--1576Approved IFCC recommendation on reporting results for blood glucose (abbreviated).512005electrochemistry methodology biosensor theory In current clinical practice, plasma and blood glucose are used interchangeably with a consequent risk of clinical misinterpretation. In human blood, glucose, like water, is distributed between erythrocytes and plasma. The molality of glucose (amount of glucose per unit of water mass) is the same throughout the sample, but the concentration is higher in plasma because the concentration of water and, therefore, glucose is higher in plasma than in erythrocytes. Different devices for the measurement of glucose may detect and report fundamentally different quantities. Different water concentrations in calibrators, plasma, and erythrocyte fluid can explain some of the differences. Results of glucose measurements depend on sample type and on whether methods require sample dilution or use biosensors in undiluted samples. If the results are mixed up or used indiscriminately, the differences may exceed the maximum allowable error of glucose determinations for diagnosing and monitoring diabetes mellitus, and complicate the treatment. The goal of the IFCC Scientific Division Working Group on Selective Electrodes and Point of Care Testing (IFCC-SD, WG-SEPOCT) is to reach a global consensus on reporting results. The document recommends reporting the concentration of glucose in plasma (with the unit mmol/L), irrespective of sample type or measurement technique. A constant factor of 1.11 is used to convert concentration in whole blood to the equivalent concentration in the pertinent plasma. The conversion will provide harmonized results, facilitating the classification and care of patients and leading to fewer therapeutic misjudgments.http://www.bibsonomy.org/bibtex/232c079afecaea573afbb6cdb0c340c2c/biblio24biblio242006-07-07T01:10:50+02:00immunoassay methodology statistic ag_detection antibody <span style="color:#555555;">Ajit <a href="http://www.bibsonomy.org/author/Sadana">Sadana</a> and Aruna M. <a href="http://www.bibsonomy.org/author/Beelaram">Beelaram</a> </span><em>Biosensors and Bioelectronics</em><em>10(3-4):301--316</em>(<em>1995</em>)Fri Jul 07 01:10:50 CEST 2006Biosensors and Bioelectronics3-4301--316Antigen-antibody diffusion-limited binding kinetics of biosensors: a fractal analysis101995immunoassay methodology statistic ag_detection antibody A fractal analysis is made of antigen-antibody binding kinetics in various biosensor applications reported in the literature. Both sensor configurations are considered, wherein (a) the antigen is in solution and the antibody is immobilized on the fibre-optic surface, and (b) the antibody is in solution and the antigen is immobilized of the fibre-optic surface. For example when the antigen is immobilized, an increase in the fractal dimension value (anti-Ars) in solution leads to (a) an increase in the fractal dimension value and hence the state of disorder or roughness, and (b) a higher rate coefficient for binding on the fibre-optic surface. An analysis of the influence of different parameters on the fractal dimension values for a particular effect, such as a comparison of fresh and regenerated immunosensors, helps to clarify the conformational states and reactions occurring on the fibre-optic surface. Examination of the different cases presented together provides novel physical insights into the state of disorder or roughness on the surface. This research should contribute towards techniques for manipulating the reactions occuring on fibre-optic surfaces in desired directions.http://www.bibsonomy.org/bibtex/22595b4e43dcf61d24ff9e5992c792ea9/biblio24biblio242006-07-07T01:10:50+02:00competition immunosensor statistic ag_detection methodology <span style="color:#555555;">Claudio <a href="http://www.bibsonomy.org/author/Domenici">Domenici</a> and Antonio <a href="http://www.bibsonomy.org/author/Schirone">Schirone</a> and Michele <a href="http://www.bibsonomy.org/author/Celebre">Celebre</a> and Arti <a href="http://www.bibsonomy.org/author/Ahluwalia">Ahluwalia</a> and Danilo De <a href="http://www.bibsonomy.org/author/Rossi">Rossi</a> </span><em>Biosensors and Bioelectronics</em><em>10(3-4):371--378</em>(<em>1995</em>)Fri Jul 07 01:10:50 CEST 2006Biosensors and Bioelectronics3-4371--378Development of a TIRF immunosensor: modelling the equilibrium behaviour of a competitive system101995competition immunosensor statistic ag_detection methodology In this work a number of instrumental aspects related to different optical configurations of Total Internal Reflection Fluoresence (TIRF) systems are introduced, and the influence of some biological reaction parameters on the performance of optical TIRF immunosensors are discussed.The manner in which fundamental quantities, such as the dissociation constant of the immunological reaction in the adsorbed phase, affect the measurement range of a TIRF immunosensor is described. The effects of light scattering at the interface and non-specific binding are also examined.Using a simple equilibrium model, in which experimental values of the surface density of active antibodies and of the dissociation constants in the immobilized phase are used, these parameters are directly related to the range of concentrations in which a competitive immunosensor gives a useful response. It is shown that amongst the most critical parameters affecting sensor performance are the dissociation constant of the antibody-antigen and antibody-labelled antigen reactions in the immobilized phase. Methods of controlling the effects of these parameters are considered.http://www.bibsonomy.org/bibtex/2add144424f8ef132fe1bf753e6b5f3c3/biblio24biblio242006-07-07T01:10:50+02:00immunosensor methodology statistic <span style="color:#555555;">Sandra F. <a href="http://www.bibsonomy.org/author/Feldman">Feldman</a> and Egidijus E. <a href="http://www.bibsonomy.org/author/Uzgiris">Uzgiris</a> and John <a href="http://www.bibsonomy.org/author/Y.">Y.</a> and <a href="http://www.bibsonomy.org/author/Gui">Gui</a> and Emily Y. <a href="http://www.bibsonomy.org/author/Shu">Shu</a> and Edward B. <a href="http://www.bibsonomy.org/author/Stokes">Stokes</a> </span><em>Biosensors and Bioelectronics</em><em>10(5):423--434</em>(<em>1995</em>)Fri Jul 07 01:10:50 CEST 2006Biosensors and Bioelectronics5423--434Evanescent wave immunoprobe with high bivalent antibody activity101995immunosensor methodology statistic We have determined the kinetic response of an evanescent wave optical fibre immunosensor and its absolute sensitivity. Using both kinetic methods and optical determinations of bound antigen, we infer that there are 2[middle dot]4 x 1011 active antibodies per cm2 probe area. We estimate that 75% of the active antibodies are in the bivalent form, with both binding site capable of binding antigen. Using the kinetic data and optical measurements of the number of antigens bound to the fibre, we estimate that the unstirred dead layer thickness next to the fibre surface in the stirred solution, across which the antigens must diffuse, is 55 [mu]m. Approximately 109 FITC labelled antigens are necessary to achieve a threshold signal, defined as 1% of the signal obtained when the fibre is saturated with antigen.http://www.bibsonomy.org/bibtex/2ae12ca63e5b1998fcd27a36718d9e650/biblio24biblio242006-07-07T01:10:50+02:00antibody methodology ag_detection homogeneous immunosensor biosensor statistic <span style="color:#555555;">J. R. <a href="http://www.bibsonomy.org/author/Astles">Astles</a> and W. G. <a href="http://www.bibsonomy.org/author/Miller">Miller</a> </span><em>Analytical Chemistry</em><em>66(10):1675--1682</em><em>May1994. </em>Fri Jul 07 01:10:50 CEST 2006Department of Pathology, Medical College of Virginia, Virginia Commonwealth University, Richmond 23298-0597.Analytical ChemistryMay101675--1682Measurement of free phenytoin in blood with a self-contained fiber-optic immunosensor.661994antibody methodology ag_detection homogeneous immunosensor biosensor statistic We describe the measurement of the anticonvulsant drug phenytoin (5,5-diphenylhydantoin) in human blood and plasma using a self-contained fiber-optic immunosensor which gave a reversible response to changes in concentration. No regenerative treatment of the immunosensor was required between measurements. The analytical signal depended on the degree of energy transfer from B-phycoerythrin labeled with phenytoin to Texas Red labeled anti-phenytoin antibody. Dextran 70K was added to the reagent system to equalize the oncotic pressure across the encapsulation membrane. A gas chromatography reference method was used to measure free drug concentrations. Regression analysis for plasma samples gave the relationship (sensor) = 1.02 (reference) + 0.07 microM; Syx = 1.00 microM; r = 0.953; sensor mean 4.45 microM; reference mean 4.31 microM. Sensor performance in plasma and whole blood was essentially equivalent. We demonstrate the feasibility of measuring free phenytoin directly in blood and suggest that the sensor design is generally applicable for the measurement of other haptens in blood.http://www.bibsonomy.org/bibtex/2af61277e530185c46d4f97c82aa3b634/biblio24biblio242006-07-07T01:10:50+02:00immunoassay antibody statistic methodology <span style="color:#555555;">H. <a href="http://www.bibsonomy.org/author/Nygren">Nygren</a> and M. <a href="http://www.bibsonomy.org/author/Werthen">Werthen</a> and M. <a href="http://www.bibsonomy.org/author/Stenberg">Stenberg</a> </span><em>J Immunol Methods</em><em>101(1):63--71</em><em>July1987. </em>Fri Jul 07 01:10:50 CEST 2006J Immunol MethodsJuly163--71Kinetics of antibody binding to solid-phase-immobilised antigen. Effect of diffusion rate limitation and steric interaction.1011987immunoassay antibody statistic methodology The binding of monoclonal antibodies to surface-immobilised antigen was studied. Antibodies against dinitrophenyl-benzene and O6-ethyl-2'-deoxyguanosine with a known affinity for the antigen were used. The amount of bound antibodies was measured by ellipsometry with an accuracy of +/- 0.15 pmol/cm2, and a sensitivity of 0.11 pmol/cm2. The binding rate of the initial antibody binding could become diffusion rate limited, and the binding rate at surface concentrations above 1 pmol/cm2 was affected by steric interaction between bound antibodies. Bound antibodies did not dissociate when rinsed with saline for up to 20 h, but dissociated in the presence of antigen (0.1 mM). The dissociation rate did not follow any identifiable rate constant. The results are discussed in relation to theoretical models of the kinetics of antigen-antibody reactions at solid-liquid interfaces.http://www.bibsonomy.org/bibtex/2782529e9a465eed9ea4b8a32781c5c3a/biblio24biblio242006-07-07T01:10:50+02:00methodology antibody immunoassay review statistic <span style="color:#555555;">H. <a href="http://www.bibsonomy.org/author/Nygren">Nygren</a> and M. <a href="http://www.bibsonomy.org/author/Stenberg">Stenberg</a> </span><em>Immunology</em><em>66(3):321--327</em><em>March1989. </em>Fri Jul 07 01:10:50 CEST 2006Department of Histology, University of Göteborg.ImmunologyMarch3321--327Immunochemistry at interfaces.661989methodology antibody immunoassay review statistic The immunochemistry of antibody binding to solid-phase immobilized antigen is reviewed. Experimental data are compared with different theoretical models of reaction mechanisms at solid-liquid interfaces. It was found that reactions at the solid-liquid interface can become limited by the diffusion rate due to depletion of reactants close to the surface, even though the intrinsic bimolecular reaction at the surface is reaction-rate limited. The forward reaction-rate constant decreases with increasing concentration of bound antibodies at the surface, and when not limited by diffusion the forward reaction rate can be more than 1000-fold slower than the corresponding reaction in a liquid solution. Possible explanations for this phenomenon are discussed. The dissociation of bound antibodies is a slow process at solid phases. The antigen-antibody complexes formed are practically irreversible. Some evidence is presented which indicates that the stability of these complexes can be due to attractive lateral interactions between bound antibodies.http://www.bibsonomy.org/bibtex/2e85834afbb22ec3be66dda6b5e9b51c2/biblio24biblio242006-07-07T01:10:50+02:00immunoassay antigen review antibody binding methodology <span style="color:#555555;">J. E. <a href="http://www.bibsonomy.org/author/Butler">Butler</a> </span><em>Methods</em><em>22(1):4--23</em><em>September2000. </em>Fri Jul 07 01:10:50 CEST 2006Interdisciplinary Immunology Training Program, University of Iowa, Iowa City, Iowa 52242, USA.MethodsSeptember14--23Solid supports in enzyme-linked immunosorbent assay and other solid-phase immunoassays.222000immunoassay antigen review antibody binding methodology A very large proportion of modern immunoassays involve the use of synthetic solid phases to immobilize one of the reactants. These solid-phase immunoassays (SPIs) therefore involve ligand-receptor interactions that occur within a reaction volume close to the solution/solid phase interface. As a consequence, the immunochemistry/biochemistry of these ligand-receptor interactions differs from that of their counterparts in solution. Furthermore, the immobilization process can significantly alter the biological activity of the reactant; most adsorbed proteins on polystyrene or silicone are partially or largely denatured. Therefore the use of alternative methods of immobilization is attractive but may result in little increase in the amount of total functional reactant. However, all commonly used solid phases do not have the same properties or the same capacity for reactant immobilization or experience the same level of nonspecific binding. Empiricism plays a major role in SPIs. Derivations of mass law equations for measuring the antigen capture of solid-phase antibodies, for determining the affinity of solid phase for protein adsorption, and for estimating antibody affinity are reviewed.http://www.bibsonomy.org/bibtex/286342add6fd708f25e1a9b72b1a5eabf/biblio24biblio242006-07-07T01:10:50+02:00antigen methodology kinetic review binding immunoassay antibody <span style="color:#555555;">A. <a href="http://www.bibsonomy.org/author/Sadana">Sadana</a> and A. B. <a href="http://www.bibsonomy.org/author/Ram">Ram</a> </span><em>Appl Biochem Biotechnol</em><em>60(2):123--138</em><em>August1996. </em>Fri Jul 07 01:10:50 CEST 2006Chemical Engineering Department, University of Mississippi, University 38677-9740, USA.Appl Biochem BiotechnolAugust2123--138Antigen-antibody binding kinetics for biosensors. Changes in the fractal dimension (surface roughness) and in the binding rate coefficient.601996antigen methodology kinetic review binding immunoassay antibody The diffusion-limited binding kinetics of antigen in solution to antibody immobilized on a biosensor surface is analyzed within a fractal framework. Changes in the fractal dimension, Df observed are in the same and in the reverse directions as the forward binding rate coefficient k. For example, an increase in the concentration of the isoenzyme human creatine kinase isoenzyme MB form (CK-MB) (antigen) solution from 0.1 to 50 ng/mL and bound to anti-CK-MB antibody immobilized on fused silica fiber rods leads to increases in the fractal dimension Df from 0.294 to 0.5080, and in the forward binding rate coefficient k from 0.1194 to 9.716, respectively. The error in the fractal dimension Df decreases with an increase in the CK-MB isoenzyme concentration in solution. An increase in the concentration of human chorionic gonadotrophin (hCG) in solution from 4000 to 6000 mIU/mL hCG and bound to anti-hCG antibody immobilized on a fluorescence capillary fill device leads to a decrease in the fractal dimension Df from 2.6806 to 2.6164, and to an increase in the forward binding rate coefficient k from 3.571 to 4.033, respectively. The different examples analyzed and presented together indicate one means by which the forward binding rate coefficient k may be controlled, that is by changing the fractal dimension or the "disorder' on the surface. The analysis should assist in helping to improve the stability, the sensitivity, and the response time of biosensors.http://www.bibsonomy.org/bibtex/2ea1a25e78f75fa76c9ef3131f268bcc4/biblio24biblio242006-07-07T01:10:50+02:00binding antigen antibody methodology immunoassay review <span style="color:#555555;">J. E. <a href="http://www.bibsonomy.org/author/Butler">Butler</a> </span><em>Methods Mol Med</em>(<em>2004</em>)Fri Jul 07 01:10:50 CEST 2006Department of Microbiology, Interdisciplinary Immunology Training Program, The University of Iowa, Iowa City, USA.Methods Mol Med333--372Solid supports in enzyme-linked immunosorbent assay and other solid-phase immunoassays.942004binding antigen antibody methodology immunoassay review Most modern immunoassays involve the use of synthetic solid phases to immobilize one of the reactants, often by simple adsorption. These solid-phase immunoassays (SPIs) involve ligand-receptor interactions that occur within a reaction volume close to the solution/solid-phase interface. As a consequence, the immunochemistry/biochemistry of these ligand-receptor interactions differ from their counterparts in solution. Nevertheless, mass law equations can be derived for measuring the antigen capture of solid-phase antibodies, for determining the affinity of solid phases for protein adsorption, and for estimating antibody affinity. Many proteins adsorbed on polystyrene or silicone suffer adsorption-induced conformational changes (ACC) and are partially or largely denatured. Alternative methods for immobilizing proteins and virus, while preserving antigenicity, may yield only a modest increase in functional reactant concentration. Peptides and small recombinant proteins appear to benefit especially from nonadsorptive immobilization. Not all solid phases commonly used in SPIs have the same properties, the same capacity for reactant immobilization, cause the same level of denaturation, or experience the same level of nonspecific binding. Empiricism, adherence to a few practical rules of thumb, and avoidance of certain "old wives tales" can be valuable in the successful development of SPIs.http://www.bibsonomy.org/bibtex/2fe6ee91c9cf344ac0ed56047180650f0/biblio24biblio242006-07-07T01:10:50+02:00displacement methodology ag_detection statistic <span style="color:#555555;">S. Y. <a href="http://www.bibsonomy.org/author/Rabbany">Rabbany</a> and A. W. <a href="http://www.bibsonomy.org/author/Kusterbeck">Kusterbeck</a> and R. <a href="http://www.bibsonomy.org/author/Bredehorst">Bredehorst</a> and F. S. <a href="http://www.bibsonomy.org/author/Ligler">Ligler</a> </span><em>J Immunol Methods</em><em>168(2):227--234</em><em>February1994. </em>Fri Jul 07 01:10:50 CEST 2006Department of Engineering, Hofstra University, Hempstead, NY 11550.J Immunol MethodsFebruary2227--234Effect of antibody density on the displacement kinetics of a flow immunoassay.1681994displacement methodology ag_detection statistic This study investigates the effect of antibody density on the kinetics of a solid-phase displacement immunoassay. Conducted in flow under nonequilibrium conditions, the assay utilizes a monoclonal antibody to the cocaine metabolite benzoylecgonine, which has been immobilized onto Sepharose beads and saturated with fluorophore labeled antigen. Displacement of antibody-bound labeled antigen by non-labeled antigen occurs when sample is introduced in the buffer flow. Comparison of matrices coated with two different antibody densities revealed that the displacement efficiency is a function of the density of antibody-bound labeled antigen. A higher density of antibody provides a higher amount of displaced labeled antigen, but the displacement efficiency of the assay is decreased. The effect of antibody density on the immunoassay kinetics was analyzed using a mathematical formulation developed to characterize antibody-antigen interactions at solid-liquid interfaces. Higher antibody density proved to be associated with a lower apparent dissociation rate constant. The implications of these results on the design of immunoassays in flow are discussed.