Relevant bibliographies by topics / Reaction affinity

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Reaction affinity'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 February 2022

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Journal articles on the topic "Reaction affinity"

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Pekař, Miloslav. "Affinity and Reaction Rates: Reconsideration of Theoretical Background and Modelling Results." Zeitschrift für Naturforschung A 64, no. 5-6 (June 1, 2009): 289–99. http://dx.doi.org/10.1515/zna-2009-5-602.

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Abstract The phenomenological affinity approach to chemical kinetics based on mass-action rate expression is revised. It is shown that the reaction rate is not an unambiguous function of affinity and that in ideal mixtures with only elementary reactions thermodynamic coupling, i. e. a positive reaction rate and negative affinity of some reaction step at the same time, is not possible. Neither does thermodynamic coupling occur in a non-ideal system of elementary reactions where the mass-action rate equation is written with activities in place of concentrations. The non-ideality and/or non-equality of reaction orders to stoichiometric coefficients lead to more complex affinity-rate relationships than commonly given which puts no explicit restrictions on affinity and rate signs. Theoretical considerations are completed with results of numerical modelling made on several simple mechanisms. Various combinations of affinity and rate signs and complex affinity-rate profiles were obtained. Modelling results support the idea that affinity is much more a result of the time evolution of a reacting system and corresponding time profiles of concentrations than the actual cause of reaction rates.
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Rakitzis, E. T. "Utilization of the free energy of the reversible binding of protein and modifying agent towards the rate-enhancement of protein covalent modification." Biochemical Journal 269, no. 3 (August 1, 1990): 835–38. http://dx.doi.org/10.1042/bj2690835.

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An analysis is presented of the catalytic factors responsible for the rate-enhancement that may be observed when a protein modification reaction is compared with a reaction of the same modifying agent with a model micromolecular compound exhibiting the same reactive group as the protein under study. It is seen that affinity-mediated rate-enhancement of protein modification is realized by the loss of activation entropy. On the assumption that attainment of maximal affinity-mediated rate-enhancement presents with an activation entropy of the protein modification reaction equal to zero, whereas the activation enthalpy of the reaction remains unchanged, it is shown that the value for maximal affinity-mediated rate-enhancement is equal to e-delta s++/R. Accordingly, protein modification reactions may be differentiated into (i) reactions the rate-enhancement of which (relative to the reaction of the same modifying agent with a model compound) is primarily entropy-controlled and (ii) reactions the rate-enhancement of which is primarily enthalpy-controlled. It is seen that modifying agents of low reactivity towards model compounds, but with a high, i.e. highly negative, activation entropy are better suited as prospective affinity-based protein-modifying agents, since the potential affinity-mediated rate-enhancement, and hence the selectivity, of these compounds is necessarily high. Kinetic and thermodynamic constants of the reaction of modifying agents with proteins, and with model compounds, and values of maximal affinity-mediated rate-enhancement, based on published data of the reaction of several modifying agents with model compounds, are presented and discussed.
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Hall, Denver G. "Reaction Rate, Activities and Affinity — Further Comments." Zeitschrift für Physikalische Chemie 153, Part_1_2 (January 1987): 213–16. http://dx.doi.org/10.1524/zpch.1987.153.part_1_2.213.

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PATTISON, D. R. M., C. DE CAPITANI, and F. GAIDIES. "Petrological consequences of variations in metamorphic reaction affinity." Journal of Metamorphic Geology 29, no. 9 (July 18, 2011): 953–77. http://dx.doi.org/10.1111/j.1525-1314.2011.00950.x.

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Pekař, Miloslav. "Affinity and Reaction Rates: Reconsideration of Experimental Data." Helvetica Chimica Acta 90, no. 10 (October 2007): 1897–916. http://dx.doi.org/10.1002/hlca.200790198.

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Caoili, Salvador Eugenio C. "On the Meaning of Affinity Limits in B-Cell Epitope Prediction for Antipeptide Antibody-Mediated Immunity." Advances in Bioinformatics 2012 (November 14, 2012): 1–17. http://dx.doi.org/10.1155/2012/346765.

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B-cell epitope prediction aims to aid the design of peptide-based immunogens (e.g., vaccines) for eliciting antipeptide antibodies that protect against disease, but such antibodies fail to confer protection and even promote disease if they bind with low affinity. Hence, the Immune Epitope Database (IEDB) was searched to obtain published thermodynamic and kinetic data on binding interactions of antipeptide antibodies. The data suggest that the affinity of the antibodies for their immunizing peptides appears to be limited in a manner consistent with previously proposed kinetic constraints on affinity maturation in vivo and that cross-reaction of the antibodies with proteins tends to occur with lower affinity than the corresponding reaction of the antibodies with their immunizing peptides. These observations better inform B-cell epitope prediction to avoid overestimating the affinity for both active and passive immunization; whereas active immunization is subject to limitations of affinity maturation in vivo and of the capacity to accumulate endogenous antibodies, passive immunization may transcend such limitations, possibly with the aid of artificial affinity-selection processes and of protein engineering. Additionally, protein disorder warrants further investigation as a possible supplementary criterion for B-cell epitope prediction, where such disorder obviates thermodynamically unfavorable protein structural adjustments in cross-reactions between antipeptide antibodies and proteins.
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Keeble, Anthony H., Paula Turkki, Samuel Stokes, Irsyad N. A. Khairil Anuar, Rolle Rahikainen, Vesa P. Hytönen, and Mark Howarth. "Approaching infinite affinity through engineering of peptide–protein interaction." Proceedings of the National Academy of Sciences 116, no. 52 (December 10, 2019): 26523–33. http://dx.doi.org/10.1073/pnas.1909653116.

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Much of life’s complexity depends upon contacts between proteins with precise affinity and specificity. The successful application of engineered proteins often depends on high-stability binding to their target. In recent years, various approaches have enabled proteins to form irreversible covalent interactions with protein targets. However, the rate of such reactions is a major limitation to their use. Infinite affinity refers to the ideal where such covalent interaction occurs at the diffusion limit. Prototypes of infinite affinity pairs have been achieved using nonnatural reactive groups. After library-based evolution and rational design, here we establish a peptide–protein pair composed of the regular 20 amino acids that link together through an amide bond at a rate approaching the diffusion limit. Reaction occurs in a few minutes with both partners at low nanomolar concentration. Stopped flow fluorimetry illuminated the conformational dynamics involved in docking and reaction. Hydrogen–deuterium exchange mass spectrometry gave insight into the conformational flexibility of this split protein and the process of enhancing its reaction rate. We applied this reactive pair for specific labeling of a plasma membrane target in 1 min on live mammalian cells. Sensitive and specific detection was also confirmed by Western blot in a range of model organisms. The peptide–protein pair allowed reconstitution of a critical mechanotransmitter in the cytosol of mammalian cells, restoring cell adhesion and migration. This simple genetic encoding for rapid irreversible reaction should provide diverse opportunities to enhance protein function by rapid detection, stable anchoring, and multiplexing of protein functionality.
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Girr, Philipp, Jessica Kilper, Anne-Christin Pohland, and Harald Paulsen. "The pigment binding behaviour of water-soluble chlorophyll protein (WSCP)." Photochemical & Photobiological Sciences 19, no. 5 (2020): 695–712. http://dx.doi.org/10.1039/d0pp00043d.

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Alison-Youel, Sarah D. "Observation and Analysis of Affinity Law Deviations through Tested Performance of Liquefied Gas Reaction Turbines." International Journal of Rotating Machinery 2008 (2008): 1–5. http://dx.doi.org/10.1155/2008/737285.

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Liquefied gas reaction turbines are subject to the hydraulic affinity laws. Particularly for liquefied hydrocarbon gas-driven turbines, deviations from the affinity laws are encountered. In the case of reaction turbines, where the geometry is fixed, the affinity law relationships between flow, head, and rotational speed are relevant. Field experience confirms that the affinity law relationships are adequate, but that the predictions made also tend to deviate from real turbine performance. Part of the deviations seen may be attributed to the nonideal fluid; however, further examination is warranted. This paper presents an investigation into the affinity law relationships between head, flow, and rotational speed in conjunction with actual turbine performance. The three basic affinity law relationships are combined to form the most general performance equation. This equation subsequently incorporates both the affinity law relationships and the conservation of energy principal. Application of real turbine test data shows that this general performance equation presents a more accurate representation of turbine performance than the affinity law relationships alone.
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Sakamoto, Keiichi, Satoru Yoshino, Makoto Takemoto, Kazuhiro Sugaya, Hitomi Kubo, Tomoe Komoriya, Shinnosuke Kamei, and Shigeki Furukawa. "Synthesis of arylsulfanyl-subphthalocyanines and their ring expansion reaction." Journal of Porphyrins and Phthalocyanines 19, no. 05 (May 2015): 688–94. http://dx.doi.org/10.1142/s1088424615500194.

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For dye-sensitized solar cells, phthalocyanines require strong absorption of far-red light between 700 and 850 nm because of their high electron transfer efficiency. Nevertheless phthalocyanines lack of affinity to basal plats, they inhibit utilization as dye-sensitized solar cell photosensitizer. Then, subphthalocyanines are used as precursors to prepare asymmetric 3:1 type phthalocyanines using a ring-enlargement technique to give affinity to basal plates. As subphthalocyanines having arylsulfanyl substituents used as a precursor, asymmetric phthalocyanines are expected to have good affinity to basal plates. Spectroscopic properties and electron transfer abilities to synthesize non-peripheral arylsulfanyl-subphthalocyanines were estimated. In addition to prepare as trial, asymmetric 3:1 type phthalocyanine, hexakis[(4-methylphenyl)thio]phthalocyanine, was synthesized from corresponding subphthalocyanine.
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Dissertations / Theses on the topic "Reaction affinity"

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Haigh, Jonathan Michael. "Novel affinity ligands for immunoglobulins based on the multicomponent Ugi reaction." Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599837.

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A novel use of the four-component Ugi reaction to generate a solid-phase, immunoglobulin-binding library is described herein. An aldehyde-functionalised Sepharose solid-support constituted one component in the four-component reaction, whereas the other three components (a carboxylic acid, a primary or secondary amine and an isonitrile) were varied in a combinatorial fashion to generate the final tri-substituted scaffold structure which provides a degree of rigidity and functionality suitable for rational investigation of immunoglobulin binding. The Ugi ligand library was initially screened chromatographically against whole human IgG and fragmented (Fc and Fab) molecules. A number of putative lead candidates emerged for whole IgG, in addition to highly specific Fab and Fc-binding ligands. A Fab-specific ligand (A3C1I1) comprising an Ugi scaffold substituted with 1-amino-2-naphthol (A3), glutaric acid (C1) and isopropyl isocyanide (I1) was selected based on its ability to bind Fab differentially over Fc. Preparative chromatography of IgG from human plasma showed 100% of serum IgG was adsorbed from the 20 mg ml-1 crude stock and subsequently eluted with a purity of 81.0% under non-optimised conditions. High purity Fab and IgG isolation was achieved from both yeast and E. coli host cell proteins. The lead candidate was modelled in silico and docked into a human Fab fragment (PDB: 1AQK) to suggest a putative binding interface to the constant CH1-CL Fab terminal through six defined hydrogen bond interactions together with putative hydrophobic interactions. The immobilised ligand was subjected to a series of studies to define an optimised affinity adsorbent which binds 73.06 mg IgG ml-1 moist gel (dynamic binding capacity at 10% breakthrough) and a static binding capacity of 16.1 ± 0.25 mg Fab ml-1 moist resin displaying an affinity constant Kd: (2.6 ± 0.3) x 10-6 M.
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Chen, Chen. "Affinity ligands for glycoprotein purification based on the multicomponent Ugi reaction." Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.709063.

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Brown, Alec J. "Ipsative Score Distortion on Affinity 2.0." Diss., CLICK HERE for online access, 2005. http://contentdm.lib.byu.edu/ETD/image/etd1119.pdf.

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O'Malley, Patrick Daniel. "Development and Application of Reaction Route Graph Representation and Analysis of Catalytic Reaction Networks." Digital WPI, 2017. https://digitalcommons.wpi.edu/etd-dissertations/534.

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Chemical reactions can have a staggering amount of molecular complexity. Reaction mechanisms have been proposed with over one hundred elementary reaction steps that occur in the same system simultaneously. While several methods exist to simplify and make sense of the pathways and kinetics via which these reactions proceed, e.g., reaction graphs, sensitivity or flux analysis, microkinetic analysis, and comparison of energy landscapes, etc., these methods all have limitations and are often not able to capture a comprehensive picture of the kinetics of system. It has been found useful to view these mechanisms as a network, i.e., a reaction graph. These graphs enable the visualization of the pathways of the reaction and can provide an analytical tool for pathway and kinetic analysis. However, many of the specific graph-theoretic approaches in the literature are not the most suitable for kinetic analysis of complex mechanisms; as they are simply not based on rules that are rigorous enough to fully enumerate all the pathways or provide quantitative analysis of the reaction rates. Our Reaction Route (RR) Graph approach is different in that it depicts the mechanism by a graph that is consistent with all physical and chemical laws associated with reaction networks, particularly being consistent with mass and energy conservation, i.e., Kirchoff’s Flux Law (KFL) and Kirchoff’s Potential Law (KPL). Because of their adherence to these laws, RR Graphs are able to provide an accurate graph-theoretical tool not only for depicting all reactions routes as walks (hence the name RR Graph) but also for pruning mechanisms and allowing a simplified but accurate quantitative description of reaction rates. This adherence to KFL and KPL does mean that the construction and implementation of these graphs can be prohibitively difficult for large mechanisms. For large reaction systems,especially nonlinear mechanisms, it is not realistic to generate these graphs by hand. And although there exists an analytical solution to find a determinant matrix for the RR Graph of a mechanism, the process involves an exhaustive search for a solution which experiences a combinatorial explosion as the number of steps gets very large. This leads to the idea of developing an algorithm for a computer program that can determine how to generate these graphs automatically. Unfortunately, the same combinatorial explosion is present such that for a moderately sized twenty step mechanism, it could take an average computational processor over a decade to find a solution. We have determined, however, that this brute force combinatorial approach can be avoided if heuristics could be developed to bridge gaps in our knowledge of how these graphs are constructed. Thus, developing a better analytical approach and/or a tighter set of heuristics for a computer algorithm are the overarching goals of this work. To make progress toward developing such heuristics, a set of microkinetic mechanisms were analyzed with the notion that the realization of the RR Graphs would highlight a better approach to their construction and usage. In particular, a very large linear reaction system, a smaller linear system and two non-linear reaction systems were analyzed to develop insights into how each graph is manually constructed and analyzed. Furthermore, kinetic analysis was done for these mechanisms and compared to experimental data and other analytical tools to prove not only the validity of the RR Graphs, but also how they are a significant improvement over more commonly used approaches for mechanistic and kinetic analysis. Based on the lessons learned through a consideration of these examples, a set of heuristics are established and enumerated with the ultimate goal of developing an intuitive algorithm that can help automate drawing and kinetic analysis via RR Graphs of complex mechanisms.
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Ng, Kheng Tee. "Novel synthetic affinity ligands based on an Ugi multicomponent reaction for the purification of human antibodies." Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.709427.

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Kaleta, Erin. "Applications of mass spectrometry to bacterial diagnostics: Affinity capture matrix assisted laser desorption/ionization mass spectrometry and polymerase chain reaction mass spectrometry." Diss., The University of Arizona, 2011. http://hdl.handle.net/10150/305352.

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This dissertation presents the application of mass spectrometry to the detection and characterization of microorganisms based on biomarker identification and DNA analysis. Two major topics are covered: affinity capture mass spectrometry using immunoassay methods and methods involving insertion of membrane receptors into polymerized planar supported lipid bilayers; and the application of mass spectrometry for use in clinical microbiology for the identification of microorganisms causing bloodstream infections. Affinity capture mass spectrometry on immunoassay-based platforms studied the capture of Protein A from Staphylococcus aureus , demonstrating capture that is both selective and sensitive. Experiments illustrated successful capture from a purified source and cell lysates. Affinity capture using receptors inserted into polymerized lipid bilayers was also performed using GM1 and cholera toxin subunit B, demonstrating the enhanced stability offered by polymerizing the lipid bilayers such that direct ionization could be performed. Detection of protein binding was achieved with mass spectrometry at low molar ratios of receptor, and enzymatic digestion experiments on the protein retained at the surface illustrated the ability to characterize the protein ligand bound, lending support to using this technique for reverse pharmacological applications. Lastly, experiments demonstrated that affinity capture of surface-bound proteins can also be used to extract cells from complex mixture prior to the polymerase chain reaction, illustrating utility as a pre-treatment for detecting microorganisms in blood samples. Mass spectrometry was applied to detection of microorganisms from blood culture bottles collected from patients with bloodstream infections. Polymerase chain reaction electrospray ionization and whole cell matrix-assisted laser desorption/ionization mass spectrometry were used to characterize hematopathogens. High diagnostic accuracy was demonstrated with respect to culture-based testing and these two platforms were compared considering accuracy in identification, time to result, and cost benefit analysis. The experiments presented here cover a broad range of detection strategies for identifying proteins and microorganisms. The affinity capture techniques describe the first application of peptide capture and polymerized bilayers for mass spectrometric analysis, and the clinical mass spectrometry work demonstrates validation of two emerging techniques and the first comparative study on both platforms simultaneously. All research presented here demonstrates promise for application of mass spectrometry in diagnostic biology.
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Barman, Jharna. "Targeting RNA by the Antisense Approach and a Close Look at RNA Cleavage Reaction." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis Acta Universitatis Upsaliensis, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-8272.

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Brundin, Malin. "Stability of bacterial DNA in relation to microbial detection in teeth." Doctoral thesis, Umeå universitet, Institutionen för odontologi, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-82735.

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The fate of DNA from dead cells is an important issue when interpreting results from root canal infections analysed by the PCR technique. DNA from dead bacterial cells is known to be detectable long time after cell death and its stability is dependent on many different factors. This work investigated factors found in the root canal that could affect the recovery of microbial DNA. In an ex vivo experiment, DNA from non-viable gram-positive Enterococcus faecalis was inoculated in instrumented root canals and recovery of DNA was assessed by PCR over a two-year period. DNA was still recoverable two years after cell death in 21/25 teeth. The fate of DNA from the gram-negative bacteria Fusobacterium nucleatum and the gram-positive Peptostreptococcus anaerobius was assessed in vitro. DNA from dead F. nucleatum and P. anaerobius could be detected by PCR six months post cell death even though it was clear that the DNA was released from the cells due to lost of cell wall integrity during the experimental period. The decomposition rate of extracellular DNA was compared to cell-bound and it was evident that DNA still located inside the bacterium was much less prone to decay than extracellular DNA. Free (extracellular) DNA is very prone to decay in a naked form. Binding to minerals is known to protect DNA from degradation. The fate of extracellular DNA was assessed after binding to ceramic hydroxyapatite and dentine. The data showed that free DNA, bound to these materials, was protected from spontaneous decay and from enzymatic decomposition by nucleases. The main conclusions from this thesis were: i) DNA from dead bacteria can be detected by PCR years after cell death ex vivo and in vitro. ii) Cell-bound DNA is less prone to decomposition than extracellular DNA. iii) DNA is released from the bacterium some time after cell death. iv) Extracellular DNA bound to hydroxyapatite or dentine is protected from spontaneous decomposition and enzymatic degradation.
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陳磊碩 and Lui-sek Chan. "Chemical modification of immunoglobulins and the effects on antigen binding site affinity." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1993. http://hub.hku.hk/bib/B29913378.

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Chan, Lui-sek. "Chemical modification of immunoglobulins and the effects on antigen binding site affinity /." [Hong Kong] : University of Hong Kong, 1993. http://sunzi.lib.hku.hk/hkuto/record.jsp?B13731506.

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Books on the topic "Reaction affinity"

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1964-, Yang Xueming, and Liu Kopin, eds. Modern trends in chemical reaction dynamics. Singapore: World Scientific, 2004.

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(Editor), Xueming Yang, and Kopin Liu (Editor), eds. Modern Trends In Chemical Reaction Dynamics: Experiment And Theory (Advanced Series in Physical Chemistry). World Scientific Publishing Company, 2004.

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Larsen, Timothy. The Hope That is in You. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198753155.003.0013.

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The focus of this chapter is on the posthumously published Three Essays on Religion: ‘Nature’, ‘Utility of Religion’, and ‘Theism’. The contents of all three are presented, including Mill’s addressing the problem of evil by denying divine omnipotence while affirming the goodness of God, his probabilist theism, his case for reasonable hope, and for the divine mission of Jesus Christ. There is also a discussion of Mill’s affinity with the Broad Church and liberal Anglicanism. Finally, there is a presentation of the negative reaction to ‘Theism’ by disciples of Mill who were religious unbelievers such as Alexander Bain and John Morley.
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Hughes, Emily. Studying Talk to Her. Liverpool University Press, 2015. http://dx.doi.org/10.3828/liverpool/9781906733438.001.0001.

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Talk to Her (2002) is a hugely rich and interesting, though ambiguous, film that met with both popular success and critical acclaim. The film won an Oscar for best original screenplay and has been hailed by some critics as Pedro Almodóvar's masterpiece. Yet like most of Almodóvar's films, little is clear-cut. The characters are complex and our affinity and empathy for them shifts throughout the film. This book provides an in-depth analysis of both the formal elements of the film (its narrative, genre, and auteur study) and the themes and issues it raises, discussing the social context of modern Spain and its old, traditional iconography; shifting attitudes towards gender; and, crucially, the film's uneasy, morally ambiguous depiction of rape and the spectator's reaction to it.
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Book chapters on the topic "Reaction affinity"

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de Berg, Kevin C. "The Reaction: Chemical Affinity and Controversy." In The Iron(III) Thiocyanate Reaction, 31–39. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-27316-3_4.

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de Berg, Kevin C. "The Reaction: Chemical Affinity: Laws, Theories and Models." In The Iron(III) Thiocyanate Reaction, 41–52. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-27316-3_5.

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Tuerk, Craig, Sheela MacDougal-Waugh, Gerald Z. Hertz, and Larry Gold. "In Vitro Evolution of Functional Nucleic Acids: High-Affinity RNA Ligands of the HIV-1 rev Protein." In The Polymerase Chain Reaction, 233–43. Boston, MA: Birkhäuser Boston, 1994. http://dx.doi.org/10.1007/978-1-4612-0257-8_20.

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El Khoury, Graziella, Laura A. Rowe, and Christopher R. Lowe. "Biomimetic Affinity Ligands for Immunoglobulins Based on the Multicomponent Ugi Reaction." In Chemical Genomics and Proteomics, 57–74. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-349-3_5.

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Freidin, A. B., I. K. Korolev, S. P. Aleshchenko, and E. N. Vilchevskaya. "Chemical Affinity Tensor and Chemical Reaction Front Propagation: Theory and FE-Simulations." In Defect and Material Mechanics, 119–33. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-51632-5_10.

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Kalosaka, Katerina, W. F. Beck, G. Brudvig, and G. Cheniae. "Coupling of the PS2 Reaction Center to the O2-Evolving Center Requires a Very High Affinity Ca2+ Site." In Current Research in Photosynthesis, 721–24. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_164.

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Mazzanti, B., E. Traggiai, B. Hemmer, R. Martin, L. Massacesi, and M. Vergelli. "The affinity spectrum of myelin basic protein-reactive T cells." In Advances in the Immunopathogenesis of Multiple Sclerosis, 3–9. Milano: Springer Milan, 1999. http://dx.doi.org/10.1007/978-88-470-2269-0_2.

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Wang, Cunxi, Thomas C. Lee, Kathleen S. Crowley, and Erin Bell. "One-Step Purification of Phosphinothricin Acetyltransferase Using Reactive Dye-Affinity Chromatography." In Methods in Molecular Biology, 35–42. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2447-9_3.

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Ambrosius, D., S. Bala-Mohan, C. Behrendt, K. Schäfer, A. Schüttler, and D. Brandenburg. "NEW PHOTO-REACTIVE DERIVATIVES OF INSULIN FOR AFFINITY-LABELLING OF THE INSULIN RECEPTOR." In Porto Carras, Chalkidiki, Greece, Aug. 31–Sept. 5, 1986, edited by Dimitrios Theodoropoulos, 521–24. Berlin, Boston: De Gruyter, 1987. http://dx.doi.org/10.1515/9783110864243-122.

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Wang, Cunxi, Thomas C. Lee, Kathleen S. Crowley, and Erin Bell. "ERRATUM: Chapter 3: One-Step Purification of Phosphinothricin Acetyltransferase Using Reactive Dye-Affinity Chromatography." In Methods in Molecular Biology, E1. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2447-9_26.

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Conference papers on the topic "Reaction affinity"

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Hoisch, Thomas D., Suzanne D. Craddock, and Eric D. Kelly. "EXCESS GARNET GROWTH IN METAMORPHIC ROCKS DRIVEN BY REACTION AFFINITY ASSOCIATED WITH OVERSTEPPED REACTIONS." In GSA Annual Meeting in Seattle, Washington, USA - 2017. Geological Society of America, 2017. http://dx.doi.org/10.1130/abs/2017am-300296.

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Freidin, Alexander B. "Chemical Affinity Tensor and Stress-Assist Chemical Reactions Front Propagation in Solids." In ASME 2013 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/imece2013-64957.

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We consider a stress-assist chemical reaction front propagation in a deformable solid undergoing a localized chemical reaction between solid and gas constituents. The reaction is sustained by the diffusion of the gas constituent through the transformed solid material. We introduce a chemical transformations strain tensor that relates two reference configurations of solid constituents. Then mass, momentum and energy balances are written down for the open system considered and the expression of the entropy production due to the reaction front propagation in a solid with arbitrary constitutive equations is derived. As a result, the expression of the chemical affinity tensor is obtained. Kinetic equation for the chemical reactions front propagation is formulated in a form of the dependence of the front velocity on normal components of the chemical affinity tensor. The locking effect — blocking the reaction by stresses is demonstrated. Finally the kinetic equation for the bulk chemical reaction is derived in a form of the dependence of the reaction rate on the first invariant of the chemical affinity tensor.
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Lee, Min-Ho, Hye Youn Kim, Young Tai Seo, and Kuk Nyung Lee. "Simple, fast, and quantitative detection of affinity reaction of osteocalcin using amperometric method." In 2014 International Conference on Information Science, Electronics and Electrical Engineering (ISEEE). IEEE, 2014. http://dx.doi.org/10.1109/infoseee.2014.6947771.

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Jackson, Craig M. "A DEFINITION OF HEPARIN ANTICOAGULANT POTENCY APPLICABLE TO ALL HEPARINS AND HEPARIN-LIKE SUBSTANCES AND ITS PRACTICAL APPLICATION IN ASSAYING HEPARIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642928.

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Heparins increase the rate of inactivation of proteinases by antithrombin without being consumed in the inactivation reaction. The anticoagulant activity of any heparin or heparin preparation is thus determined by the increase in the inactivaton rate which it produces. This rate increase is dependent on the concentration of the heparin in the sample and on some now well known structural properties of the individual heparin molecules that produce high affinity for antithrombin . All proteinases are not inactivated by antithrombin equally rapidly in the absence of heparin, nor are heparins and heparin derivatives of different molecular weight equally effective in the inactivation of the same proteinase. Under appropriate conditions, the observed rate constant (kObs) for the heparin catalyzed proteinase inactivation reaction is simply related to the intrinsic potencies and concentrations of the individual high affinity heparin molecules in the sample. The intrinsic potency of a high affinity heparin molecule is the efficiency with which it catalyzes the inactivation of the particular proteinase, e.g. Factor Xa or thrombin, i.e., it is a second order rate constant, (designated k*) . After k* has been determined from kobs for a known heparin or heparin preparation and a particular proteinase, the concentration of heparin in an unknown sample can be calculated from the equation[H] = [HAT] = kobs/k* In general terms, the appropriate conditions, i.e.,the antithrombin and proteinase concentrations, the pH, and ionic strength, required for this equation to be used are those conditions for which all of the high affinity heparin is bound to the antithrombin and pseudo first order kinetic behavior occurs. At very low heparin concentrations, a correction for the inactivation of the proteinase by antithrombin alone is necessary, but is easily made.Supported by Organon Teknika Corporation and an Established Investigator Award from the American National Red Cross
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5

Knupp, C. L. "STUDIES OF A HIGH AFFINITY, STABLE PLATELET-THROMBIN COMPLEX FORMED DURING PLATELET ACTIVATION. A POSSIBLE MECHANISM FOR TRANSMEMBRANE SIGNAL GENERATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644472.

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The precise mechanism of signal transmission from the platelet surface to the interior required for thrombin-induced platelet activation is not known. A stable complex between Iodo-[125l]-thrombin and platelets has been noted previously on SDS polyacrylamide gels. This 77,000 dalton complex was thought to represent the high affinity binding found in binding studies. The complex is inhibited by excess native thrombin but not by excess active site-modified thrombin. Thus, it displays the characteristics of the crucial thrombin-platelet interaction needed for platelet activation. My studies using similar methods for analysis were performed to determine if this interaction might have a role in signal generation for thrombin-induced platelet activation. Thrombin concentration studies with 3 minute incubations demonstrated that formation of the complex occurred only at thrombin doses which result in platelet activation (above 0.1 U/ml). The amount of the complex increased as the thrombin dose increased. Time course studies with thrombin 1 U/ml revealed that the reaction was rapid and was present on platelets after only 5 seconds of incubation. The complex was noted in supernatants but not until 30 seconds. This interaction was not present on platelets chilled to 4°C and was markedly diminished on platelets exposed to the metabolic inhibitors, antimycin A and 2-deoxyglu-cose. The specific thrombin inhibitors, hirudin and dansylargin-ine N-(3-ethyl-l,5-pentanediyl) amide, prevented the complex formation. Addition of either inhibitor after formation of the complex reversed its formation up to 1 minute after the addition of thrombin but not beyond this time. Treatment with trypsin but not chymotrypsin removed this complex from the platelet. It is concluded that this reaction is not simply a binding event as it requires functional platelets and is only formed at thrombin doses which activate platelets. It is an early, specific, surface reaction which requires thrombin binding and active-site domains for its formation. Formation of this complex is consistent with observation of "receptor processing" noted with specific thrombin binding. Therefore, this reaction could have an important function in the signal processing mechanism for thrombin-induced platelet activation.
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6

Shore, J. D., D. E. Day, and S. T. Olson. "KINETIC EFFECTS OF HIGH MOLECULAR WEIGHT KININOGEN AND ZINC ON CONTACT ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642852.

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Previous work in our laboratory showed that Zn2+ enhanced the rate of kallikrein generation by dextran sulfate (DxSO4) in dialyzed normal plasma, but not in Fitzgerald or Hageman prismas. This could be partially explained by a marked effect of Zn2+ on factor XII autoactivation, and our present work involves zinc effects on other reactions of contact activation. At physiological ionic strength (0.15 μ), the kcat/Km for Xlla activation of prekallikrein (PK) was 0.62 μM™1 s™1 which was increased to 4.35 μM™1 s™1 by the presence of 25μg/ml DxSO4. High molecular weight kininogen (HMK) at 40 nM further increased this to 10.8 μM™1 s™1 , and 5 ¼M Zn2+ had no effect. To determine whether these cofactors promote a surface-dependent activation of PK by XIIa under conditions which weaken the protein-surface interactions, the kinetics were examined at 0.3μ. At this ionic strength, kcat/Km was 0.18 μM™1 s™1 and was unchanged by 25μg/ml DxSO4. This was increased to .805 μM™1 s™1 by 150 nM HMK and further increased 10-fold to 8.35 μM™1 s™1 by 10 μM™1 Zn2+ . Qualitative results were obtained at 0.3 μ for the other reciprocal reaction, XII activation by kallikrein (K). To observe XII activation within 2 hours, both 10 μM Zn2+ and 25 μM HMK were essential, indicating that these cofactors have a very large enhancing effect on the kinetics of this reaction. Chromatography of HMWK on DxSO4-agarose ^ljiowed elution of the protein at 0.42 M NaCl in the absence of Zn2+ ,but at 0.88M in its presence, providing evidence that Zn+ markedly increases the affinity of HMK for DxSO4. Our results are consistent with the increased activation rates observed in the presence of Zn2+ and HMK due to enhanced binding affinity of the reacting proteins to surfaces. This is likely to be essential for proper function of the contact system in blood, where many other proteins compete for surface. Supported by USPHS grant HL-25670
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7

Niederst, P. N., M. Asbach, M. Ott, and R. E. Zimmermann. "IN VITRO REACTION MODELS OF THROMBIN AND ITS PHYSIOLOGICAL INHIBITOR ANTITHROMBIN III IN THE PRESENCE OF HEPARIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644356.

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Antithrombin III (AT III) neutralizes thrombin and other serine proteases of plasma coagulation system by forming a stable 1:1 covalent complex. The inhibition rates are greatly increased by the potent catalyst heparin. The catalytic mechanism of heparin was studied in the presence of dextran sulfate (DS), a thrombin-binding sulfated Polysaccharid. DS did not influence the reaction of AT III with heparin and the amidolytic activity of thrombin, but preincubation with thrombin could inhibit the catalytic activity of heparin in the reaction of thrombin with AT III. We conclude that the reaction of heparin with enzyme and inhibitor, thus forming a ternary complex, is necessary for its catalytic activity.It is known that heparin also converts AT III from an inhibitor to a substrate for thrombin in a dose dependent manner. By cleavage of the reaction site bound Arg(385)-Ser(386) an AT III-fragment (MG 50000 d) occurs, which has a decreased affinity to heparin and does not inhibit F I la. At physiological ionic strength we have only measured a small percentage of AT 111-proteolysis (4%, 1 U/ml Hep). The extent of AT III-fragment formation could be enhanced by lowering the ionic strength (max 44%, 1 U/ml Hep., 1=0,02).
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8

Xia, Hui, Bobby Mathew, Hisham Hegab, and June Feng. "Simulation Based Optimization of Microfluidic Devices Used for Molecular Enrichment." In ASME 2012 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/imece2012-88324.

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Microfluidic devices are used in several engineering fields ranging from biomedical to chemical to engineering for applications such as micro reactor, target molecular enriching and cell capturing. With regard to related applications, microfluidic devices offer advantages such as high surface area to volume ratio, increased mass transfer coefficient and portability in addition to their requirement of low analytes. Affinity based microfluidic devices with microscale posts have high compactness and mass transfer coefficient. In order to maximize the benefits offered by employing microfluidic devices, it is important to apply parametric study in the device designing work. This study is aimed at studying the operating and geometric parameters of microfluidic devices with square/rectangular microscale posts. The geometric parameters, such as aspect ratio of the microposts used, could possibly decide the performance of the device. Operating parameters studied are Reynolds number, Peclet number, Damköhler number, and equilibrium reaction constant. These parameters encompass the influence of velocity, diffusivity, density, viscosity, hydraulic diameter, inlet concentration of species and absorption/desorption reaction constants. This work theoretically analyzes the influence of the above mentioned parameters using COMSOL Multiphysics 4.2.a. The governing equations of microfluidic devices, i.e. Navier-Stokes equations and the advection-diffusion equation, subjected to the above mentioned operating parameters, are solved to obtain the velocity profile, pressure drop and concentration profile of the species. The metric used for analyzing the influence of each operating parameter is the capture efficiency, i.e. the ratio of outlet concentration to inlet concentration as well the pressure drop. The results of this study would improve the design of microfluidic devices used for chemical reactions as well as that used for protein enrichment.
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9

Olson, Steven T., Ingemar Bjork, Paul A. Craig, Joseph D. Shore, and Jean Choay. "ROLE OF THE HIGH-AFFINITY PENTASACCHARIDE IN HEPARIN ACCELERATION OF ANTITHROMBIN III INHIBITION OF THROMBIN AND FACTOR Xa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642829.

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The high-affinity heparin pentasaccharide (H5) and an 8000 Mr high-affinity heparin (H26) have been compared with respect to their interaction with antithrombin III (AT) and their accelerating effect on AT inhibition of thrombin (T) and factor Xa by rapid kinetic and equilibrium binding studies at pH 7.4, 25°C. Kds of .068 μM at I 0.15 and 0.57 μM at I 0.3 were determined for tne AT-H5 interaction, which were 5 and 2.5-fold weaker, respectively, than affinities determined for H26. Comparison of the kinetics of binding of H5 and H26 to AT at I 0.15 under pseudofirst order conditions ([H]o>> [AT]o) demonstrated a saturable dependence of the observed rate constant for both reaction with indistinguishable limiting rate constants of 700 +/-120 s-1 and 520 +/-90 s-1 , but somewhat different Kds for the initial binding interaction of 20 and 29 μM for H5 and H26, respectively. These results indicate that H5 induces the same conformational change in AT as the larger heparin, but that the rate of reversal of this conformational change is greater for H5 which is the basis for its weaker AT affinity. Bimolecular rate constants for neutralization of factor Xa and thrombin by AT-H5 and AT-H26 complexes were determined by p-aminobenzamidine displacement under pseudo-first order conditions([AT-H] >> [T]o or [Xa]o). I-in-dependent values of .62 μM-1 s-1 were obtained for Xa inhibition by AT-H5 at I 0.15 and 0.3, compared to I-dependent values of 1.4 and 0.91 μM-1 s-1 for AT-H26. For thrombin inhibition by AT-H5, and I-independent enhancement of 1.6-fold in the bimolecular rate constant from .0098 to .016 μM-1 s-1 was observed, in sharp contrast to the marked I-independent enhancement by AT-H26 of the bimolecular rate constant ranging from 4000 to 200-fold at I 0.15 and 0.3, respectively. These results are consistent with a primary ionic strength-independent contribution of the AT conformational change to heparin enhancement of factor Xa but not thrombin neutralization by AT, with an ionic strength-dependent component for both reactions, compatible with a differential role for a protease-heparin interaction. Supported by grant HL-30237
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10

Mardiguian, J., M. Corgier, and M. Jouany. "STRUCTURE ACTIVITY RELATIONSHIPS OF DERMATAN SULFATE : EFFECT OF MOLECULAR SIZE AND CARBOXYL GROUP ESTERIFICATION ON HEPARIN C0FACT0R-II ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644354.

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Dermatan is a high molecular weight glycosaminoglycan which has been shown to enhance the inhibition of thrombin by heparin-cofactor II. The aim of this study was to establish the influence of the molecular size and the role of the carboxyl group on the in vitro activity of Dermatan Sulfate. Pig skin Dermatan Sulfate was fractionated according to molecular size by gel-chromatography on Ultrogel Ac 44. Each fraction was characterized by its sulfur content and by its mean molecular weight measured on a TSK - 4000 column in reference to standard heparin fractions. Methyl esters of the unfractionated Dermatan Sulfate with varying degree of esterification, where prepared via activation of the carboxyl groups with a carbodiimide and reaction with methanol. The results of this study show that the heparin - cofactor II mediated anti-thrombin activity of Dermatan Sulfate is increasing with the molecular weight and is abolished by esterification of the carboxyl groups. Moreover, it can be speculated that each fraction contains the same amount of high affinity fraction and that, like heparin, the potency of the high affinity component is increasing with the molecular weight.
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Reports on the topic "Reaction affinity"

1

Dove, P. M., and J. P. Icenhower. Quantifying silica reactivity in subsurface environments: Controls of reaction affinity and solute matrix. 1998 annual progress report. Office of Scientific and Technical Information (OSTI), June 1998. http://dx.doi.org/10.2172/13539.

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2

Patricia M. Dove. Quantifying Silica Reactivity in Subsurface Environments: Reaction Affinity and Solute Matrix Controls on Quartz and SiO2 Glass Dissolution Kinetics. Office of Scientific and Technical Information (OSTI), December 2000. http://dx.doi.org/10.2172/791682.

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3

Dove, Patricia M. Quantifying Silica Reactivity in Subsurface Environments: Reaction Affinity and Solute Matrix Controls on Quartz and SiO2 Glass Dissolution Kinetics. Office of Scientific and Technical Information (OSTI), June 1999. http://dx.doi.org/10.2172/827365.

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4

Dove, P. M. Quantifying silica reactivity in subsurface environments: Reaction affinity and solute matrix controls on quartz and SiO{sub 2} glass. 1997 annual progress report. Office of Scientific and Technical Information (OSTI), October 1997. http://dx.doi.org/10.2172/13538.

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