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Relevant bibliographies by topics / Equilibrium dissociation and inhibition constant

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Academic literature on the topic 'Equilibrium dissociation and inhibition constant'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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Journal articles on the topic "Equilibrium dissociation and inhibition constant"

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Lindhout, T., G. Willems, R. Blezer, and H. C. Hemker. "Kinetics of the inhibition of human factor Xa by full-length and truncated recombinant tissue factor pathway inhibitor." Biochemical Journal 297, no. 1 (1994): 131–36. http://dx.doi.org/10.1042/bj2970131.

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The inhibition equilibrium and kinetics of association and dissociation of the binding of three types of recombinant tissue factor pathway inhibitor (TFPI), namely full-length TFPI, C-terminal-truncated TFPI, and TFPI without the third Kunitz domain (TFPI1-161), to factor Xa have been measured. Formation and dissociation of the complexes were monitored by continuous measurement of the changes in the rate of hydrolysis of a peptidyl-p-nitroanilide substrate. Progress curves of product formation were fitted to a set of equations describing a one-step bimolecular inhibitory reaction in the presen

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Raines, Douglas E., and Vinu T. Zachariah. "Isoflurane Increases the Apparent Agonist Affinity of the Nicotinic Acetylcholine Receptor by Reducing the Microscopic Agonist Dissociation Constant." Anesthesiology 92, no. 3 (2000): 775–85. http://dx.doi.org/10.1097/00000542-200003000-00021.

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Background Isoflurane increases the apparent agonist affinity of ligand-gated ion channels. This action reflects a reduction in the receptor's agonist dissociation constant and/or the preopen/open channel state equilibrium. To evaluate the effect of isoflurane on each of these kinetic constants in the nicotinic acetylcholine receptor, the authors analyzed isoflurane's actions on (1) the binding of the fluorescent agonist Dns-C6-Cho to the nicotinic acetylcholine receptor's agonist self-inhibition site and (2) the desensitization kinetics induced by the binding of the weak partial agonist suber

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Lobaugh, L. A., and P. J. Blackshear. "Neuropeptide Y binding and inhibition of cAMP accumulation in human neuroepithelioma cells." American Journal of Physiology-Cell Physiology 258, no. 5 (1990): C913—C922. http://dx.doi.org/10.1152/ajpcell.1990.258.5.c913.

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The specific binding of 125I-labeled neuropeptide Y (NPY) and the biological response to NPY receptor activation were measured in cultured human neuroepithelioma (SK-N-MC) cells. A single class of high-affinity binding sites [dissociation constant (KD) = 0.2 nM] was characterized both by equilibrium binding of 125I-NPY concentrations less than 1 nM and kinetically by the initial rates of 125I-NPY association and dissociation. Specific 125I-NPY binding was decreased in a concentration-dependent manner by inclusion of guanine nucleotides in the incubation medium. The existence of multiple affini

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Brown, Nicholas G., Dar-Chone Chow, and Timothy Palzkill. "BLIP-II Is a Highly Potent Inhibitor of Klebsiella pneumoniae Carbapenemase (KPC-2)." Antimicrobial Agents and Chemotherapy 57, no. 7 (2013): 3398–401. http://dx.doi.org/10.1128/aac.00215-13.

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ABSTRACTβ-Lactamase inhibitory protein II (BLIP-II) is a potent inhibitor of class A β-lactamases. KPC-2 is a class A β-lactamase that is capable of hydrolyzing carbapenems and has become a widespread source of resistance to these drugs for Gram-negative bacteria. Determination of association and dissociation rate constants for binding between BLIP-II and KPC-2 reveals a very tight interaction with a calculated (koff/kon) equilibrium dissociation constant of 76 fM (76 × 10−15M).

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Boudier, C., and J. G. Bieth. "Oxidized mucus proteinase inhibitor: a fairly potent neutrophil elastase inhibitor." Biochemical Journal 303, no. 1 (1994): 61–68. http://dx.doi.org/10.1042/bj3030061.

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N-chlorosuccinimide oxidizes one of the methionine residues of mucus proteinase inhibitor with a second-order rate constant of 1.5 M-1.s-1. Cyanogen bromide cleavage and NH2-terminal sequencing show that the modified residue is methionine-73, the P′1 component of the inhibitor's active centre. Oxidation of the inhibitor decreases its neutrophil elastase inhibitory capacity but does not fully abolish it. The kinetic parameters describing the elastase-oxidized inhibitor interaction are: association rate constant kass. = 2.6 x 10(5) M-1.s-1, dissociation rate constant kdiss. = 2.9 x 10(-3) s-1 an

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Martin, G. E. M., N. G. Rutherford, P. J. F. Henderson, and A. R. Walmsley. "Kinetics and thermodynamics of the binding of forskolin to the galactose-H+ transport protein, GalP, of Escherichia coli." Biochemical Journal 308, no. 1 (1995): 261–68. http://dx.doi.org/10.1042/bj3080261.

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The binding of the transport inhibitor, forskolin, to the galactose-H+ symporter, GalP, of Escherichia coli was evaluated by equilibrium and time-resolved fluorescence measurements. A quench in protein fluorescence of 8-12% was observed upon the binding of forskolin. The overall dissociation constant (Kd) for forskolin determined by fluorescence titration ranged between 1.2 and 2.2 microM, which is similar to that reported from equilibrium dialysis measurements of the binding of [3H]forskolin (Kd = 0.9-1.4 microM). The kinetics of forskolin binding were measured by stopped-flow fluorescence me

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Faller, B., S. Dirrig, M. Rabaud, and J. G. Bieth. "Kinetics of the inhibition of human pancreatic elastase by recombinant eglin c. Influence of elastin." Biochemical Journal 270, no. 3 (1990): 639–44. http://dx.doi.org/10.1042/bj2700639.

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Recombinant eglin c is a potent reversible inhibitor of human pancreatic elastase. At pH 7.4 and 25 degrees C, kass. = 7.3 x 10(5) M-1.s-1, kdiss. = 2.7 x 10(-4) s-1 and Ki = 3.7 x 10(-10) M. Stopped-flow kinetic indicate that the formation of the stable enzyme-inhibitor complex is not preceded by a fast pre-equilibrium complex or that the latter has a dissociation constant greater than 0.3 microM. The elastase-eglin c complex is much less stable at pH 5.0 and 25 degrees C, where kdiss. = 1.1 x 10(-2) s-1 and Ki = 7.3 x 10(-8) M. At pH 7.4 the activation energy for kass. is 43.9 kJ.mol-1 (10.5

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KAPOOR, Mili, C. Chandramouli REDDY, M. V. KRISHNASASTRY, Namita SUROLIA, and Avadhesha SUROLIA. "Slow-tight-binding inhibition of enoyl-acyl carrier protein reductase from Plasmodium falciparum by triclosan." Biochemical Journal 381, no. 3 (2004): 719–24. http://dx.doi.org/10.1042/bj20031821.

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Triclosan is a potent inhibitor of FabI (enoyl-ACP reductase, where ACP stands for acyl carrier protein), which catalyses the last step in a sequence of four reactions that is repeated many times with each elongation step in the type II fatty acid biosynthesis pathway. The malarial parasite Plasmodium falciparum also harbours the genes and is capable of synthesizing fatty acids by utilizing the enzymes of type II FAS (fatty acid synthase). The basic differences in the enzymes of type I FAS, present in humans, and type II FAS, present in Plasmodium, make the enzymes of this pathway a good targe

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Wang, Jiangnan, Jeffrey B. Velotta, Alicia A. McDonough та Robert A. Farley. "All human Na+-K+-ATPase α-subunit isoforms have a similar affinity for cardiac glycosides". American Journal of Physiology-Cell Physiology 281, № 4 (2001): C1336—C1343. http://dx.doi.org/10.1152/ajpcell.2001.281.4.c1336.

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Three α-subunit isoforms of the sodium pump, which is the receptor for cardiac glycosides, are expressed in human heart. The aim of this study was to determine whether these isoforms have distinct affinities for the cardiac glycoside ouabain. Equilibrium ouabain binding to membranes from a panel of different human tissues and cell lines derived from human tissues was compared by an F statistic to determine whether a single population of binding sites or two populations of sites with different affinities would better fit the data. For all tissues, the single-site model fit the data as well as t

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Ayre, E. A., H. Yuan, and S. F. Pang. "The identification of 125I-labelled iodomelatonin-binding sites in the testes and ovaries of the chicken (Gallus domesticus)." Journal of Endocrinology 133, no. 1 (1992): 5–11. http://dx.doi.org/10.1677/joe.0.1330005.

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ABSTRACT The existence of 125I-labelled iodomelatonin-binding sites in chicken ovaries and testes was investigated. The specific binding of 125I-labelled iodomelatonin to chicken ovarian and testicular tissue satisfies all the criteria for a binding site. It was rapid, stable, saturable, reversible, specific and of high affinity. Equilibrium studies showed that total and non-specific binding increased over a range of 5–150 pmol 125I-labelled iodomelatonin/1 tested, with specific binding reaching saturation towards the middle range of radioligand concentrations. Scatchard analyses indicated a d

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Dissertations / Theses on the topic "Equilibrium dissociation and inhibition constant"

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Gottschalk, Ingo. "Chromatographic Studies of Solute Interactions with Immobilized Red Blood Cells and Biomembranes." Doctoral thesis, Uppsala University, Department of Biochemistry, 2002. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-2668.

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<p>Specific and non-specific interactions of solutes with immobilized biomembranes were studied using chromatographic methods. Liposomes, proteoliposomes and red blood cell (RBC) membrane vesicles were immobilized by a freeze-thawing procedure, whereas whole RBCs were adsorbed in the gel beds using electrostatic interaction, binding to wheat germ agglutinin (WGA) or the streptavidin-biotin interaction. </p><p>Superporous agarose gel with coupled WGA was the most promising matrix for RBC adsorption and allowed frontal chromatographic analyses of the cells for about one week. Dissociation consta

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Lagerquist, Hägglund Christine. "Affinity-, Partition- and Permeability Properties of the Human Red Blood Cell Membrane and Biomembrane Models, with Emphasis on the GLUT1 Glucose Transporter." Doctoral thesis, Uppsala University, Department of Biochemistry, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3525.

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<p>The human glucose transporter GLUT1 is abundant in red blood cells, the blood-brain barrier and epithelial cells, where it mediates the transport of the energy metabolite, glucose. In the present work some properties of GLUT1, including affinity binding of both substrates and inhibitors, transport rates as well as permeabilities of aromatic amino acids and drug-membrane interactions were analyzed by chromatographic methods.</p><p>Reconstitution by size-exclusion chromatography on Superdex 75 from a detergent with a low CMC that provides monomeric GLUT1 was examined regarding D-glucose- and

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Neubauer, Svetlana. "Untersuchungen von inter- und intramolekularen Interaktionen des globalen Regulators AbrB und dessen Antirepressors AbbA." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2014. http://dx.doi.org/10.18452/16887.

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Aus den frühen Bindungsstudien des globalen Regulators AbrB mit der ausgedehnten phyC-Promotorregion von Bacillus amyloliquefaciens FZB45 konnte ein mehrstufiger kooperativer Bindungsprozess abgeleitet werden. Dabei verlangt die AbrB-vermittelte Repression von phyC nach Integrität zweier großer Bindungsstellen, ABS1 und ABS2, die 162 bp voneinander entfernt liegen. In der vorliegenden Arbeit wurden die ersten Echtzeitkinetiken zur DNA-AbrB-Interaktion mittels der Oberflächenplasmonresonanz (SPR) gemessen und analysiert. AbrB zeigte hohe Affinitäten zu den 40 bp langen Oligonukleotiden, die de

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Jeřábková, Kateřina. "Vliv dlouhodobého podávání morfinu na opioidní receptory v mozkové kůře potkana." Master's thesis, 2012. http://www.nusl.cz/ntk/nusl-307435.

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-5- ABSTRACT A huge effort has been put in determining the mechanism of the development of tolerance and dependence in context of clinical use of morphine for treatment of severe pain. Understanding of this mechanism would help to design new and more efficient pharmaceuticals. This diploma paper discus the opiate receptors with a special focus on long-term effect of chronic morphine treatment, which was determined using a radioligand binding assays with a non-selective antagonist [3 H]Diprenorphine. One of the goals of this work was to create and optimise a method for preparation of pure plasm

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Book chapters on the topic "Equilibrium dissociation and inhibition constant"

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Ellenbroek, Bart, Alfonso Abizaid, Shimon Amir, et al. "Equilibrium Dissociation Constant." In Encyclopedia of Psychopharmacology. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_796.

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Nigrovic, Vladimir, Ashraf Banoub, and Frank G. Standaert. "The Roles of the Equilibrium Dissociation Constant and the Receptor Concentration on the Time Course of Neuromuscular Block." In Muscle Relaxants. Springer Japan, 1995. http://dx.doi.org/10.1007/978-4-431-66896-1_98.

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"Equilibrium Dissociation Constant." In Encyclopedia of Psychopharmacology. Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-36172-2_200282.

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"Equilibrium Dissociation Constant (Kd)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_5490.

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Johnson, Jason L., and Gregory D. Reinhart. "Effects of High Pressure on the Allosteric Properties of Phosphofructokinase from Escherlchia coli." In High Pressure Effects in Molecular Biophysics and Enzymology. Oxford University Press, 1996. http://dx.doi.org/10.1093/oso/9780195097221.003.0019.

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Phosphofructokinase (PFK) from Escherichia coli is subject to allosteric regulation by phosphoenolpyruvate (PEP) and MgADP. These ligands inhibit and activate, respectively, by binding to a single allosteric binding domain and thereby altering the affinity the enzyme displays for its substrate, fructose-6-phosphate (Fru-6-P). The effect of hydrostatic pressure of up to 1.4 kbar on the binding of each of these ligands to PFK has been evaluated. This pressure range is insufficient to cause significant dissociation of the PFK tetramers. However, the logarithm of the equilibrium constant for each ligand binding to free enzyme decreases in a linear manner, and to virtually the same extent, when pressure is increased from 1 to 700 bar. Consequently, the ΔV associated with the binding of the inhibitor ligand PEP is virtually identical to the ΔV for the binding of the activator ligand MgADP or the substrate Fru-6-P, which falls within the range of 40–45 ml mol−1. The apparent ΔV for Fru-6-P binding decreases with increasing concentration of PEP until it is equal to +18 ml mol when PEP is fully saturating. Similarly, ΔV for Fru-6-P binding decreases to +26 ml mol−1 when MgADP is fully saturating. These data are interpreted as implying that both PEP and MgADP improve the “fit” of Fru-6-P to its binding domain despite the fact that the ligands have opposing effects on Fru-6-P binding affinity. Phosphofructokinase (PFK) from E. coli is a prototypical allosteric enzyme which was one of the first to be studied in depth (Blangy & Buc, 1967; Blangy et al., 1968) after Monod et al. (1965) published their famous proposal that allosteric behavior results from the concerted transition between discrete functional states of a protein (the MWC two-state model). PFK from E. coli is a tetrameric enzyme with a single allosteric binding domain that can bind either the activator MgADP or the inhibitor PEP. Under many circumstances the substrate, fructose 6-phosphate (Fru-6-P), binds to the enzyme with positive cooperativity, and the affinity and cooperativity that Fru-6-P exhibits is modulated by the allosteric ligands in classic K-type fashion.

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Ross, John, Igor Schreiber, and Marcel O. Vlad. "Introduction to Chemical Kinetic Processes." In Determination of Complex Reaction Mechanisms. Oxford University Press, 2006. http://dx.doi.org/10.1093/oso/9780195178685.003.0004.

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It is useful to have a brief discussion of some kinetic processes that we shall treat in later chapters. Some, but not all, of the material in this chapter is presented in [1] in more detail. A macroscopic, deterministic chemical reacting system consists of a number of different species, each with a given concentration (molecules or moles per unit volume). The word “macroscopic” implies that the concentrations are of the order of Avogadro’s number (about 6.02 × 1023) per liter. The concentrations are constant at a given instant, that is, thermal fluctuations away from the average concentration are negligibly small (more in section 2.3). The kinetics in many cases, but far from all, obeys mass action rate expressions of the type . . . dA/dt = k(T )AαBβ . . . (2.1) . . . where T is temperature, A is the concentration of species A, the same for B, and possibly other species indicated by dots in the equation, and α and β are empirically determined “orders” of reaction. The rate coefficient k is generally a function of temperature and frequently a function of T only. The dependence of k on T is given empirically by the Arrhenius equation . . . k(T ) = C exp−Ea/RT (2.2) . . . where C, the frequency factor, is either nearly constant or a weakly dependent function of temperature, and Ea is the activation energy. Rate coefficients are averages of reaction cross-sections, as measured for example by molecular beam experiments. The a priori calculation of cross-sections from quantum mechanical fundamentals is extraordinarily difficult and has been done to good accuracy only for the simplest trimolecular systems (such as D + H2). A widely used alternative approach is based on activated complex theory. In its simplest form, two reactants collide and form an activated complex, said to be in equilibrium. One degree of freedom of the complex, a vibration, is allowed to lead to the dissociation of the complex to products, and the rate of that dissociation is taken to be the rate of the reaction.

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Conference papers on the topic "Equilibrium dissociation and inhibition constant"

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Zamarrón, C. "BINDING OF NATIVE PLASMINOGEN TO FIBRIN AND TO SOME FI BRINOGEN/FIBRIN DERIVATIVES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644832.

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In the fibrinolytic process: (a) fibrin provides a surface on which the major reactions of fibrinolysis occurs: the conversion of plasminogen to plasmin, the cleavage of fibrin by plasmin and the inhibition of plasmin by α2-antiplasmin, (b) some fibrinogen derivatives (e.g. the cyanogen bromide digested fibrinogen fragment denominated FCB-2) can exert stimulatory properties on the plasminogen activation and (c) the initial cleavage of fibrin by plasmin increases the rate conversion of plasminogen to plasmin.The purpose of the present work has been to correlate these three aspects of the fibrin

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Lanzafame, R., and M. Messina. "Fuels Characterization for Use in Internal Combustion Engines." In ASME 2001 Internal Combustion Engine Division Fall Technical Conference. American Society of Mechanical Engineers, 2001. http://dx.doi.org/10.1115/2001-ice-421.

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Abstract It is important provide mathematical functions able to fit with great precision experimental data on gases properties, in order to obtain reliable results when computerized models on IC engines are used. On the basis of experimental data on equilibrium constants (for dissociation phenomena occurring during combustion process in IC engines) new mathematical functions have been determined to fit experimental data. In comparison to traditional fitting polynomials, these new mathematical functions present a great accuracy in matching experimental data. These new mathematical functions hav

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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>&g

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Church, F. C., R. E. Treanor, and H. C. Whinna. "ACTIVATION OF HEPARIN COFACTOR II BY PHOSVITIN, A PHOSPHOGLYCO-PROTEIN, AND OTHER PHOSPHATE-CONTAINING POLYANIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643867.

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We are characterizing the specificity of the polyanion-binding domain of the heparin/dermatan sulfate-dependent plasma protease inhibitor, heparin cofactor II (HCII). Various phosphate-containing polyanions accelerate the HCII-catalyzed inhibition of thrombin (T). Phosvitin, a phosphoprotein, enhances the HCII/T reaction at 25°C and pH 8.0 with the apparent second-order rate constant value (K2) increasing from 5 × 104 M−1 min−1 (in the absence of phosvitin) to 8 x 10' M”1 min as phosvitin increased from 0.05 to 30 ug/ml and then decreases as phosvitin is increased above 30 ug/ml. Apparent diss

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Visser, A., I. M. A. Verhamme, D. G. Meuleman, and G. W. K. van Dedem. "AN INDIRECT KINETIC METHOD FOR ESTIMATING THE AFFINITY BETWEEN HEPARIN AND HEPARIN COFACTOR II." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644352.

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The heparin-dependent inactivation of alpha-thrombin by heparin cofactor II was studied in buffer media with a pH ranging from 6 to 9 and an ionic strength from 0.05 M to 0.80 M. We used a heparin fraction with a mean Mr of 16,000 .The log dose response curves (logarithm of the 2nd order inactivation constant vs. the logarithm of heparin concentration) display a sigmoidal behavior. The lower and upper limiting plateau and the steepness of the ascending limb are characteristic for every pH and ionic strength. Similar log dose response curves can be observed for the heparin-mediated inactivation

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Fears, R. "THE EFFECT OF HEPARIN AND FIBRIN ON THE ENZYMATIC EFFICIENCIES OF THROMBOLYTICS IN_ VITRO." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643032.

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Selective fibrinolysis may be achieved physiologically by the binding of both endogenous plasminogen activator (t-PA) and plasminogen to fibrin. It has been suggested that t-PA may also exhibit fibrin-selectivity when used at therapeutic doses for acute myocardial infarction whereas the other principal thrombo-lytics, urokinase (UK) and streptokinase (SK).plasminogen, are not bound. However, in the present kinetic studies it was found that plasminogen activation by SK.lys-plasminogen was enhanced by soluble fibrin (the effect mainly on Km), the affinity of binding to fibrin was similar to t-PA

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Lian, E. C. Y., and F. A. Siddigui. "BINDING OF 37-DKa PLATELET AGGLUTINATING PROTEIN TO HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643976.

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We have previously reported the purification of a 37-KDa platelet agglutinating protein (PAP p37) from the plasma of a patient with thrombotic thrombocytopenic purpura. using 125I-labeled p37, the properties of its binding to platelets were studied. The binding of p37 to washed human platelets from 4 normal subjects and two TTP patients after recovery was specific, concentration dependent and saturable. The Scatchard analysis revealed that the binding sites for p37 was about 100,000 per platelet with a dissociation constant of 48 × 10−9 M. The binding of p37 to erythrocytes was very little and

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Contant, G., J. L. Martinoli, and C. Thirion. "INFLUENCE OF PLASMINOGEN ACTIVATOR INHIBITOR (PAI) ON THE TISSUE PLASMINOGEN ACTIVATOR (tPA) ASSAY IN EUGLOBULIN FRACTIONS AND IN PLASMA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644861.

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Current liquid-phase methods for thedetermination of tPA in plasma involve inactivation of both tPA and plasmin inhibitors by either plasma acidificationor euglobulin fractionation. In a firststep, our liquid-phase assay was performed in euglobulin fractions (EF) and the inactivation of PAI was monitored.In a second step, we studied the influenceof PAI onthe tPA assay in plasma.When EF were used (1:10 dilution, pH 5.9), the reference curve was done with tPA (0 to 1 IU/ml) diluted in buffer.The diluted samples (tPA or EF) were incubated with fibrinogen fragments as Stimulator (0.5 mg/ml), an ex

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Sheil, Henry, and Peter Young. "Challenging the Need for Dual Gas Production Flowline Systems Using Emerging Hydrate Remediation Intervention Technology." In ASME 2011 30th International Conference on Ocean, Offshore and Arctic Engineering. ASMEDC, 2011. http://dx.doi.org/10.1115/omae2011-49191.

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Gas production flowlines are presenting flow assurance challenges in hydrate management resulting from low ambient seawater temperatures in an increasing number of deepwater developments. During operation the equilibrium hydrate temperature of the produced fluid may be above the minimum seabed temperature, and hence there is a risk of hydrate blockage in the subsea system should the hydrate inhibition system fail. The continuous injection of MEG, with little or no insulation of the subsea system, is a common hydrate mitigation strategy for a gas production system. If insufficient inhibitor is

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