Relevant bibliographies by topics / Affinity 2.0

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Affinity 2.0'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Affinity 2.0"

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Lepetit, Christine, Mogens Brøndsted Nielsen, François Diederich, and Remi Chauvin. "Aromaticity and Electron Affinity of Carbok-[3]radialenes,k=0, 1, 2." Chemistry - A European Journal 9, no. 20 (October 17, 2003): 5056–66. http://dx.doi.org/10.1002/chem.200305070.

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Beattie, J. M. A., J. P. Goss, M. J. Rayson, and P. R. Briddon. "Structure and electron affinity of silicon and germanium terminated (0 0 1)-(2 × 1) diamond surface." Journal of Physics: Condensed Matter 31, no. 39 (July 9, 2019): 395001. http://dx.doi.org/10.1088/1361-648x/ab2d6c.

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Breier, B. H., P. D. Gluckman, H. T. Blair, and S. N. McCutcheon. "Somatotrophic receptors in hepatic tissue of the developing male pig." Journal of Endocrinology 123, no. 1 (October 1989): 25–31. http://dx.doi.org/10.1677/joe.0.1230025.

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ABSTRACT The development of hepatic somatotrophic receptors and plasma concentrations of insulin-like growth factor-I (IGF-I) were investigated at five different ages (2, 20, 35, 105 and 165 days) in four male pigs per group. The specific binding of 125I-labelled porcine GH (pGH) to hepatic somatotrophic membranes was very low at 2 days of age (0·53±0·12%), and increased progressively (P <0·01) with advancing age to 3·60 ± 0·95% at 165 days of age. Specific binding of 125I-labelled bovine GH (bGH) to the same membrane preparations was markedly higher than binding of 125I-labelled pGH; it also showed a distinct developmental increase (P <0·01) with age from 4·4 ± 0·55% at 2 days of age to 24·0±1·90% at 165 days of age. Plasma concentrations of IGF-I increased significantly (P <0·01) from 79 ± 14·0 μg/l at 2 days of age to 610 ± 64·0 μg/l at 165 days of age. Non-linear regression analysis of the competitive binding data using bGH as labelled and unlabelled ligands showed linear Scatchard plots in the three youngest age groups, with an association constant (Ka) of approximately 3·5 litres/nmol. Curvilinear Scatchard plots were observed in the two oldest age groups. The Ka for the higher affinity binding site (approximately 5·0 litres/nmol) was very similar to that for the sole site observed in the younger animals. The Ka of the lower affinity binding site was approximately 0·35 litres/nmol. There was a significant (P <0·01) developmental increase in the capacity of the higher affinity binding site from 12 ± 4·6 pmol/100 mg liver at 2 days of age to 91 ± 23·0 pmol/100 mg liver at 165 days of age. These studies demonstrate heterogeneity of somatotrophic hepatic membranes in the pig and show that low concentrations of a high affinity binding site are already present in newborn pigs. A considerable developmental increase was observed in the capacity of this binding site which correlated significantly (r = 0·82, P <0·01, n = 20) with plasma concentrations of IGF-I. The role of the lower affinity binding site which was observed in addition to the high affinity binding site in older pigs is less clear. The data from the present study support the hypothesis that the postnatal rise in plasma concentrations of IGF-I is associated with the developmental increase of the capacity of the high affinity somatotrophic receptors. Journal of Endocrinology (1989) 123, 25–31
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John, W. G., and A. E. Jones. "Affinity Chromatography: A Precise Method for Glycosylated Albumin Estimation." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 22, no. 1 (January 1985): 79–83. http://dx.doi.org/10.1177/000456328502200108.

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A method is described for the estimation, in plasma, of glycosylated albumin, using the commercially available affinity chromatographic material Glycogel B (immobilised m-aminophenylboronic acid on an agarose support) to separate the glycosylated and non-glycosylated albumin, followed by the analysis of albumin concentration using rocket Immunoelectrophoresis. Glycosylated albumin and glycosylated haemoglobin showed good correlation (r=0·91) when both are estimated by affinity chromatography. The glycosylated albumin method displays good within-batch (2·8–4·4% CV) and between-batch (2·9–5·4% CV) precision, and the method is not affected by haemolysis. Using this method a reference range of 2·0–5·4% was found for glycosylated albumin. Levels of glycosylated albumin in diabetics (10·06±3·23%) were found to be significantly higher ( P<0·001) than those in non-diabetics (3·72±0·85%). It was found that loading more than 3 mg of albumin on to a 1 mL affinity column must be avoided, as this appears to overload the column.
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Janausch, Ingo G., Inma Garcia-Moreno, Daniela Lehnen, Yvonne Zeuner, and Gottfried Unden. "Phosphorylation and DNA binding of the regulator DcuR of the fumarate-responsive two-component system DcuSR of Escherichia coli." Microbiology 150, no. 4 (April 1, 2004): 877–83. http://dx.doi.org/10.1099/mic.0.26900-0.

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The function of the response regulator DcuR of the DcuSR fumarate two-component sensory system of Escherichia coli was analysed in vitro. Isolated DcuR protein was phosphorylated by the sensory histidine kinase, DcuS, and ATP, or by acetyl phosphate. In gel retardation assays with target promoters (frdA, dcuB, dctA), phosphoryl DcuR (DcuR-P) formed a high-affinity complex, with an apparent K D (app. K D) of 0·2–0·3 μM DcuR-P, and a low-affinity (app. K D 0·8–2 μM) complex. The high-affinity complex was formed only with promoters transcriptionally-regulated by DcuSR, whereas low-affinity binding was seen also with some DcuSR-independent promoters. The binding site of DcuR-P at the dcuB promoter was determined by DNase I footprinting. One binding site of 42–52 nt (position −359 to −400/−410 nt upstream of the transcriptional start) was identified in the presence of low and high concentrations of DcuR-P. Non-phosphorylated DcuR, or DcuR-D56N mutated in the phosphoryl-accepting Asp56 residue, showed low-affinity binding to target promoters. DcuR-D56N was still able to interact with DcuS. DcuR-D56N increased the phosphorylation of DcuS and competitively inhibited phosphoryl transfer to wild-type DcuR.
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BEDURFTIG, S. "Chiral, nonracemic (piperazin-2-yl)methanol derivatives with $sigma;-receptor affinity." Bioorganic & Medicinal Chemistry 12, no. 12 (June 2004): 3299–311. http://dx.doi.org/10.1016/s0968-0896(04)00264-0.

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Breier, B. H., P. D. Gluckman, and J. J. Bass. "The somatotrophic axis in young steers: influence of nutritional status and oestradiol-17β on hepatic high-and low-affinity somatotrophic binding sites." Journal of Endocrinology 116, no. 2 (February 1988): 169–77. http://dx.doi.org/10.1677/joe.0.1160169.

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ABSTRACT The binding of bovine GH (bGH) to hepatic membranes obtained from steers on either high (3% dry matter of body weight per day) or low (1% dry matter of body weight per day) planes of nutrition with or without an oestradiol-17β implant was studied (n = 5 per group). Binding studies were performed on both crude membrane homogenates and on 100 000 g microsomal membrane fractions; identical results were obtained using both preparations. In all four groups of animals, linear Scatchard plots were obtained, but following pretreatment of the membranes with MgCl2 to remove endogenously bound hormone, curvilinear plots were obtained in the groups on the high plane of nutrition. Analysis of these curves suggested the presence of a high- and low-affinity binding site, the high-affinity site being fully occupied in the absence of MgCl2 pretreatment. The specific binding of bGH in MgCl2-pretreated crude membranes was greater (P < 0·01) in well-fed steers (14·8 ± 1·6%) than in poorly fed steers (9·8 ± 0·9%). Scatchard analysis showed this to be due to the presence of a high-affinity site (dissociation constant (Kd) = 11·6 ± 3·3 pmol/l) in the well-fed animals only. In addition, there was an increase (P < 0·01) in the affinity, but not in the capacity, of the low-affinity site (Kd = 106·4 ± 22·8 pmol/l in well-fed steers and 197·0 ± 23·8 pmol/l in poorly fed steers). Oestradiol treatment was associated with an increase (P < 0·01) in specific binding at both planes of nutrition, but binding was higher (P < 0·01) in well-fed (24·8 ± 2·9%) than in poorly fed (15·6 ± 3·7%) steers. Scatchard analysis after MgCl2 pretreatment again showed a curvilinear plot at the high and a linear plot at the low nutritional plane. The effect of oestradiol was to increase (P < 0·001) the capacity of the high-affinity site from 1·87 ± 0·61 pmol/100 mg in the control well-fed group to 6·56 ± 1 ·2 pmol/100 mg. The capacity of the low-affinity site was increased (P < 0·01) from 20·1 ± 2·6 to 30·1 ± 3·2 pmol/100 mg in the well-fed group, with a similar change in the poorly fed group. Oestradiol had no effect on the apparent affinity of either binding site. These studies demonstrate a heterogeneity of somatotrophic binding sites of hepatic membranes in steers. The presence of a high-affinity site is determined by nutritional status, whereas oestradiol primarily affects receptor capacity. Thus nutrition and oestradiol have independent and qualitatively different effects on somatotrophic binding. As the rate of weight gain correlated (P < 0·01) with the capacity of the high-affinity site, it is suggested that somatotrophic receptor modulation is a primary factor in the regulation of somatic growth in the ruminant. J. Endocr. (1988) 116, 169–177
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McGrattan, P. D., A. R. G. Wylie, and J. Nelson. "Tissue-specific differences in insulin binding affinity and insulin receptor concentrations in skeletal muscles, adipose tissue depots and liver of cattle and sheep." Animal Science 71, no. 3 (December 2000): 501–8. http://dx.doi.org/10.1017/s1357729800055466.

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AbstractDifferences in insulin binding affinity and in concentrations of insulin receptor, were found in a variety of tissues taken, at slaughter, from mature steers (701 (s.d. 23) kg) and growing lambs (47 (s.d. 2·1) kg). In both species, liver had lower insulin binding affinity than skeletal muscles m. pectineus m. longissimus dorsi and m. rectus capitis (all P < 0·001) and subcutaneous, omental and perirenal adipose depots (all P < 0·001). Site-specific differences in affinity for insulin existed between adipose depots (subcutaneous < omental, P < 0·05; subcutaneous < perirenal, P < 0·001) and between tissue-types (subcutaneous fat < m. pectineus skeletal muscle, P < 0·05; m. rectus capitis < perirenal fat, P < 0·05) in steers. In lambs also, receptor affinity for insulin differed between tissue-type (m. longissimus dorsi < perirenal fat, P < 0·05; m. rectus capitis < subcutaneous fat, P < 0·05 and m. rectus capitis < perirenal fat, P < 0·001) but lambs did not show the adipose depot-specific differences in insulin affinity observed in steers. Insulin receptor concentration differed between adipose depots (subcutaneous < omental, P < 0·05; subcutaneous < perirenal, P < 0·01) and between tissue-type (m. pectineus < perirenal fat P < 0·05) in steers and perirenal and subcutaneous adipose depots of lambs had higher receptor concentrations than m. longissimus dorsi and m. pectineusP < 0·001). This is the first study to demonstrate, in any species, differences in insulin receptor binding affinity and receptor concentration in a wide range of tissues (liver, skeletal muscles and adipose depots) from the same individual. Such differences in meat-producing animals could, through effects on tissue sensitivity and/or responsiveness to insulin, influence nutrient partitioning to tissues and affect overall rates of lipid storage and net protein synthesis.
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Asai, Daisuke, Masaharu Murata, Riki Toita, Takahito Kawano, Hideki Nakashima, and Jeong-Hun Kang. "A high-affinity peptide substrate for G protein-coupled receptor kinase 2 (GRK2)." Amino Acids 51, no. 6 (April 19, 2019): 973–76. http://dx.doi.org/10.1007/s00726-019-02735-0.

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Sud’ina, A. E., T. S. Zatsepin, V. Pingoud, A. Pingoud, T. S. Oretskaya, and E. A. Kubareva. "Affinity Modification of the Restriction Endonuclease SsoII by 2′-Aldehyde-Containing Double Stranded DNAs." Biochemistry (Moscow) 70, no. 8 (August 2005): 941–47. http://dx.doi.org/10.1007/s10541-005-0206-0.

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Dissertations / Theses on the topic "Affinity 2.0"

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Ammann, Hélène. "Synthèse du N-bromométhylcétoamino-6-hexyl 0-?-D-galactopyranosyl-(l->4)-0-(acétamido-2-désoxy-2-?-D-glucopyranosyl)-(1->2)-?-D-mannopyranoside pour le marquage par affinité du site de reconnaissance des sucres chez la PHA." Mémoire, Université de Sherbrooke, 1987. http://hdl.handle.net/11143/11695.

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Les lectines sont des protéines dont les propriétés hémagglutinantes, inhibées par des sucres simples, ont attiré l'attention des chercheurs. La découverte que certaines d'entre elles, comme la phytohémagglutine (PHA), sont mitogéniques, a stimulé la recherche du mécanisme de transformation lymphoblastique. L'activation lymphocytaire induite par les lectines mitogéniques procède par la liaison de celles-ci à des récepteurs glycoprotéiques spécifiques à la surface des cellules. Bien que la structure primaire et tertiaire de quelques lectines ait été élucidée, on en connaît bien peu sur la nature des interactions avec le déterminant saccharidique. La synthèse du dérivé trisaccharidique [N-bromométhylcétoamino-6-hexyl 0-?-D-galactopyranosyl-(1->4)-0-(acétamido-2-désoxy-2-?-D-glucopyranosyl)-(1->2)-?-D-mannopyranoside] est rapportée dans le but de marquer par affinité le site de reconnaissance des sucres sur la PHA. Le choix de cet oligosaccharide est basé sur la capacité du 0-?-D-galactopyranosyl-(1->4)-0-(acétamido-2-désoxy-2-?-D-glucopyranosyl)-(1->2)-D-mannopyranose d'inhiber la stimulation lymphocytaire par la PHA [Hammarström, S., Hammarström, M.L., Sundblad, G., Arnarp, J. et Lönngren, J. (1982) Proc. Natl. Acad. Sci. USA 79, 1611-1615]. Le dérivé saccharidique protégé est obtenu par le couplage du trichloroacétimidate de 0-(tétra-0-acétyl-2,3,4,6-?-D-galactopyranosyl)-(1->4)-(tri-0-acétyl-3,4,6-désoxy-2-phtalimido-2-?-D-glucopyranoside avec le N-benzyloxycarbonylamino-6-hexyl tri-0-benzyl-3,4,6-?-D-mannopyranoside, en présence de trifluoroéthérate de bore, avec un rendement de 65%. Deux méthodes de couplage ont été initialement testées, et il s'est avéré que l'efficacité de la méthode utilisant un dérivé trichloroacétimidate du disaccharide était supérieure à celle utilisant du trifluorométhanesulfonate d'argent comme agent de condensation. Le trisaccharide ainsi obtenu a été déprotégé en suivant des procédés classiques de désacétylation, de déphtalimidation, de N-acétylation et de débenzylation. Le rendement global de déprotection du trisaccharide obtenu par couplage a été 55%. L'amine de la chaîne alkyle, libérée lors de l'hydrogénation, a été modifiée par réaction avec du bromoacétate de N-succinimidyle. Les possibilités de radiomarquage du dérivé trisaccharidique sont discutées.
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Book chapters on the topic "Affinity 2.0"

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Hage, D. S., J. A. Anguizola, R. Li, R. Matsuda, E. Papastavros, E. Pfaunmiller, M. Sobansky, and X. Zheng. "Affinity Chromatography." In Liquid Chromatography, 1–23. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-415806-1.00001-2.

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Chase, H. A. "AFFINITY SEPARATION | Biochemical Engineering Aspects Of Affinity Separations." In Encyclopedia of Separation Science, 246–52. Elsevier, 2000. http://dx.doi.org/10.1016/b0-12-226770-2/00581-0.

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Teisseire, B., C. Ropars, C. Vieilledent, and C. Nicolau. "Significance of Low Hemoglobin Oxygen Affinity." In Oxygen Transport in Red Blood Cells, 153–59. Elsevier, 1986. http://dx.doi.org/10.1016/b978-0-08-030800-5.50020-2.

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GREENE, WARNER C., YUJI WANO, and MITCHELL DUKOVICH. "New Insights into the Structure of High-Affinity Interleukin-2 Receptors." In Proceedings of the 1987 Laurentian Hormone Conference, 141–55. Elsevier, 1988. http://dx.doi.org/10.1016/b978-0-12-571144-9.50009-0.

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GABRIELSEN, ODD S., and JANINE HUET. "Magnetic DNA Affinity Purification of Yeast Transcription Factor." In Recombinant DNA Methodology II, 771–88. Elsevier, 1995. http://dx.doi.org/10.1016/b978-0-12-765561-1.50055-2.

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Moore, Pamela B., and John R. Dedman. "Calcimedins: Isolation Using Calmodulin Antagonists for Affinity Chromatography." In Calmodulin Antagonists and Cellular Physiology, 483–94. Elsevier, 1985. http://dx.doi.org/10.1016/b978-0-12-347230-4.50034-2.

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HARRIS, J. MILTON, and MANSSUR YALPANI. "Polymer-Ligands Used in Affinity Partitioning and Their Synthesis." In Partitioning in Aqueous Two-Phase System, 589–626. Elsevier, 1985. http://dx.doi.org/10.1016/b978-0-12-733860-6.50023-2.

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He, L. Z., H. Helmholz, B. Niemeyer, and X. Luo. "A diffusion model for affinity adsorption of glycoprotein on immobilized lectin." In Computational Fluid and Solid Mechanics, 1232–35. Elsevier, 2001. http://dx.doi.org/10.1016/b978-008043944-0/50884-2.

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Carson, Susan, Heather B. Miller, and D. Scott Witherow. "Extraction of Recombinant Protein from Escherichia coli Using a Glutathione Affinity Column." In Molecular Biology Techniques, 103–11. Elsevier, 2012. http://dx.doi.org/10.1016/b978-0-12-385544-2.00013-2.

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Wano, Yuji, Mitchell Dukovich, Warner C. Greene, and John H. Kehrl. "NEW PERSPECTIVES ON THE STRUCTURE OF THE HUMAN HIGH-AFFINITY INTERLEUKIN 2 RECEPTOR." In Interleukin, 99–112. Elsevier, 1988. http://dx.doi.org/10.1016/b978-0-12-651420-9.50010-5.

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Conference papers on the topic "Affinity 2.0"

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Chesney, C. M., and D. D. Pifer. "EFFECT OF Ca2+ and Mg2+ ON PLATELET ACTIVATING FACTOR (PAF) INDUCED AGGREGATION AND SPECIFIC BINDING TO HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642879.

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Gel filtered human platelets (GFP) collected in Tyrode's buffer containing 0.5 mM Ca+2, ImM Mg+2, and 0.35% albumin exhibit high affinity binding of 3H-PAF with a Kd of 0.109 α 0.029 nM (mean α SD; n=13) and 267 α 70 sites per platelet. When fibrinogen (1.67 mg/ml final concentration) is added to these GFP preparations biphasic aggregation is observed with PAF (4 nM). Normal aggregation is also observed with other platelet agonists including ADP, epinephrine, collagen, arachidonic acid, A23187 and thrombin. If GFP is prepared without added Ca+2 or Mg+2 in the presence of 3mM EDTA, platelets do not aggregate in response to PAF. However the number of specific binding sites remains unchanged (387 per platelet) with some decrease in affinity of binding (Kd = 0.2l4nM). In the presence of ImM Mg+2 there is no significant difference in binding kinetics over a range of Ca+2 concentrations (0-2mM). On the other hand the calcium channel blocker verapamil (5-10uM) exhibits competitive inhibition of 3H-PAF as analyzed by Lineweaver-Burk plots. Specific binding of 3H-PAF to GFP in the presence of ImM Mg+2 and ImM EGTA shows Kd of 0.l66nM but with increase in specific binding sites to 665. Despite increase in number of sites and no change in binding affinity, GFP under these conditions does not exhibit platelet aggregation with PAF in doses up to 80 nM.From these data it appears that external Ca+2 is not necessary for specific binding of 3H-PAF to its high affinity receptor. However, calcium does appear to be necessary for second wave aggregation with PAF. While Mg+2 appears to enhance 3H-PAF binding to platelets Mg+2 cannot substitute for Ca+2 in PAF induced platelet aggregation. Although verapamil appears to competitively inhibit binding of PAF to GFP it is not clear whether the inhibition is due to competition at or near the actual PAF receptor or at a site involving the calcium channel.
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Sakuragawa, N., T. Shimotori, and K. Takahashi. "COMPARATIVE STUDIES ON ANTITHROMBIN III AFFINITY OF LOW MOLECULAR WEIGHT HEPARIN AND UNFRACTIONATED HEPARIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644365.

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Purpose: Low molecular weight(LMW)heparin shows stronger antifactor Xa(F-Xa) and weaker anti-thrombin(TH) activities compared with unfractionated(UF) heparin, and shows less bleeding tendency in the cases of clinical use. These characteristics were surmised to be depend on antithrombin III(AT-III) affinity of the heparin. Materials and methods: LMW heparin(Kabi and Pharmuka), UF heparin (Novo) and heparin cofactor II(HC-II) purified by our method were used. AT-III affinity column chromatography with 0.1 M Tris-buffer (pH 7.4)-NaCl 0.02 to 2.5 M linear gradient was performed. From the point of AT-III affinity strength, non-affinity(Na), low affinity (La) and high affinity(Ha) were separated, and aPTT, anti-F-Xa and anti-TH activities were assayed on each fractions. HC-II was assayed by biological activity.Results: (1) Kabi-LMW heparin; Na 34.5%, La 39.3%, Ha 26.2%, Pharmuka-LMW heparin; Na 58.0%, La 24.1%, Ha 17.3%. Novo; Na 0%, La 50%, Ha 50%. (2) APTT; Na showed no effect, but Ha showed the strongest prolonging effects on aPTTs even having less amount of uronic acid, and more prominent effects were observed in UF(Novo)-heparin than LMW heparins. (3) La showed higher activity of anti-F-Xa and anti-TH activities than Ha. (4) Anti-TH activity of AT-III was observed in both fractions of La and Ha, but that of HC-II was observed in each fractions including Na.Conclusion: It was surmised that the differences of the characteristics between LMW heparin and UF heparin were depend on to the strength of AT-III. The different characteristics of HC-II from AT-III to anti-TH were observed and surmised to be depend on the binding ability to the fractions.
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Mardiguian, J. "IS PENTASACCHARIDE THE SMALLEST HEPARIN OLIGOSACCHARIDE WITH BINDING AFFINITY TO ANTITHROMBIN III ? AN OVERVIEW." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644849.

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The binding of heparin to antithrombin III is ascribed to the presence in the heparin molecule of a specific binding site which contains a typical 3-0- sulfate group located on a glucosamine residue. It has been postulated that the smallest heparin oligosaccharide capable of high affinity binding to antithrombin III and eliciting anti-factor Xa activity is a pentasaccharide containing three glucosamine units and two uronic acid residues. Such a pentasaccharide has been recently isolated after chemical depolymerization of pig mucosal heparin and its structure found to be very close to that of a synthetic pentasaccharide prepared by other investigators. However no convincing data have, so far, excluded the possibility that an oligosaccharide composed of less than five sugar units could not be able to bind to antithrombinlll and to elicit anti-factor Xa activity. We report now the isolation of new oligosaccharides obtained by beta-eliminative chemical depolymerization of heparin using three different procedures : depolymerization of heparin benzyl ester (1) in aqueous medium and (2) in non-aqueous medium: (3) alcaline depolymerization of a periodate oxydized acetyl heparin. The data reported show that the high affinity oligosaccharides isolated after affinity chromatography on immobilized antithrombin III are distinct from the previously isolated pentasaccharide and that there is some evidence that these are tetrasaccharides resulting from the cleavage of the non reducing end of the heparin molecule
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Kribben, A., E. Fritschka, M. Sibold, M. Fassbender, A. Distler, and Th Philipp. "EFFECT OF FUROSEMIDE ON PLATELET AGGREGATION AND ON ALPHA-ADRENOCEPTOR-DENSITY IN MAN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643447.

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Furosemide (FUR) reduces the ∝2-adrenoceptor- (∝2-R) mediated pressor effect of norepinephrine. Since it has been shown that FUR reduces platelet aggregation ( AGG) we studied the effect of FUR on α2-R as well as that on the ∝2-R-medi ated epinephrine ( EPI)-induced AGG a) ex vivo and b) in vitro. For comparison the effect of FUR on ADP-induced AGG was also studied. Methods: a) 8 normotensive men received FUR (30 mg b. i.d. ) for 3 weeks. EPI- (1 μmol/1) and ADP- (1 μmol/1) induced platelet AGG were measured before as well as after 3 weeks of FUR application with a semiautomatic device ( APACT) . Platelet ∝2-R-density was measured by 3H-yohimbine-binding and the fraction of high-affinity binding-sites was measured by competi tion of 3H-yohimbine with EPI. b) Platelet-rich plasma was incubated with FUR (1 mmol/1) for 10 min at 37 °C and AGG was measured (n=7) as described. Results: a) FUR decreased ∝2-R-densi ty from 293± 28 to 251±; 21 fmol/mg protein (p< 0.01) and high affinity binding sites from 64± 3 to 55± 5 % (p< 0.01). FUR inhibited ADP-induced AGG ex vivo while EPI-induced AGG did not change (table). b) In vitro FUR inhibited total ADP-induced AGG from 7 4 ± 4 to 45± 8 % (p< 0. 01) while again EPI-induced AGG did not change.Conclusions: The results suggest separate effects of FUR on α2 R-density and on platelet AGG. Although FUR decreased < r2-R, EPI-induced platelet AGG remained unchanged. Since FUR inhibited ADP-induced AGG ex vivo as well as in vitro FUR may interfere directly with the mechanism of ADP-induced platelet AGG.
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5

Hack, N., J. M. Wilkinson, and N. Crawford. "A MONOCLONAL ANTIBODY (PL/IM 430) THAT BLOCKS THE ACTIVE TRANSL0CATI0N OF Ca2+ INTO HUMAN PLATELET INTRACELLULAR MEMBRANE (ER) VESICLES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644678.

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In earlier studies [1] we identified a number of important biological properties associated with highly purified human platelet intracellular membrane (ER), isolated by continuous flow electrophoresis. These included a high affinity Ca2+Mg2+ ATPase and protein phosghorylation both of which are involved inthe active uptake of Ca into ER vesicles. The stored Ca2+ could be released with inositol(1,4,5)trisphosphate, (IP ), (approx. 50% release in 30 s 1/2 max. for release - 0.253 μM IP3,) [2]. To probe the structure-function relationship of proteins in these ER vesicles, a panel of monoclonal antibodies (Mabs) has been raised, using the ER membrane preparation as immunogen. Four of these Mabs recognise a single 100 kDa polypeptide by immunoblotting. This protein is present in platelet membranes and can also be identified in cultured human monocyte, macrophage and endothelial cell lines. None of the M^bs showed any significant effect upon the ER membrane Ca2+ Mg2+ ATPase activity but one, PL/IM 430 (of IgGl subclass), inhibited the Ca2+sequestration by the vesicles significantly (approx. 70% inhibition at 10 μM IgG). This inhibition was independent of the ATP concentration over a range2of 0-2 mM ATP, but was2dose-dependent for external free Ca 2between 30-300 nM Ca2+, giving maximum inhibition at 300 nM Ca with 10 pM IgG2+ Binding of the antibody substantially lowers the Vmax for Ca2+for Ca2+ uptake but is without effect upon the Km. PL/IM 430 therefore appears to recognise a 100 kDa polypeptide closely involved with Ca2+ trnslocation but at a site which i, s without effect upon the Ca2+Mg− ATPase associated with the Ca pump.We are grateful to the Wellcome Trust and the British Heart Foundation for financial support for these studies.[1] Hack, N., Croset, M. and Crawford, N. (1986) Biochem. J. 233, 661-668.[2] Authi, K. S. and Crawford, N. (1985) Biochem. J. Z3O, 247-253
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6

Owen, B. A., and W. G. Owen. "ASSOCIATION OF HEPARIN AND FACTOR Xa: INFLUENCE ON THE RATE OF INHIBITION OF FACTOR Xa BY ANTITHROMBIN III-HEPARIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643837.

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Association of heparin non-covalently with bovine factor Xa was analyzed by Superose-12 gel chromatography. In 0.05 M NaCl, 0.02 M Tris, pH 7.5, DEGR-Xa (factor Xa inactivated by dans-Glu-Gly-Arg-CH2Cl) was eluted as a single, sharp peak at Ve/Vt=0-65 (elution volume/internal volume). Mixtures of heparin and DEGR-Xa were eluted as two partially resolved peaks of protein at Ve/Vt=0.59 and 0.65. The fraction of DEGFUXa in the leading peak was directly proportional to [heparin], and at 100 yM heparin the leading peak contained more than half the total protein. When 0.02 M HEPES was substituted for Tris a single, slightly broadened peak at Ve/Vt=0.64 was obtained on chromatography of 100 μM heparin and 10 μM DEGR-Xa. In a buffer system comprising 0.02 M Tris, 0.02 M HEPES, 0.03 M NaCl, pH 7.5, two peaks were eluted at Ve/Vt=0.59 and 0.65. Therefore, Tris increases the affinity of DEGR-Xa for heparin.Solutions buffered with Tris or HEPES were compared for effects on the kinetics of inhibition of factor Xa by antithrombin III-heparin. Reaction mixtures containing 1 nM factor Xa, 30 nM heparin and 600 nM antithrombin III were assayed with S-2222 at intervals of 2-10 sec. Reagent concentrations were chosen (a) to assure pseudo-first-order kinetics, (b) to have [heparin]<< Kq for factor Xa-heparin, and (c) to bind virtually all available heparin to antithrombin III. The same second-order rate constant, Kobs=2.5×107 M−1s−1, was obtained in both buffer systems. We conclude that the association of factor Xa with heparin observed directly by gel chromatography does not contribute to the reaction rate of factor Xa with antithrombin III-heparin.
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7

Marcovina, S., R. Coppola, M. P. Protti, C. Gelfi, and P. M. Mannucci. "EDTA-DEPENDENT MONOCLONAL ANTIBODIES TO HUMAN PROTEIN S." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644294.

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Splenocytes from a Balb/c mouse immunized with purified human protein S (PS) were fused with murine hybridoma cell line SP2/0-Agl4 and cultured in Iscove's medium without addition of fetal bovine serum. Hybrid supernatants were screened for the presence of specific antibodies by solid-phase ELISA and cloned by the limiting dilution technique. Pour clones, named S2, S3, S8, and S10, were selected, recloned several times, and injected intraperitoneally into Balb/c mice for the production of antibody-rich ascitic fluid. The monoclonal antibodies (Mabs), all of IgGl subclass with k light chain, were purified from ascitic fluid by Protein-A chromatography. The specificity of Mabs was controlled by the immunoblotting technique: the Mabs appeared to react only with two plasma proteins, one with a MW of about 70.000 dal tons comigrating with purified PS, and the other with a MW >300.000 da that is likely to be the C4b-binding protein-PS complex. No interaction has been observed with PS-depleted plasma. As tested by a fluid phase radio immunoassay, the binding of Mabs to PS was significantly higher in the presence of EDTA while was totally inhibited in the presence of Ca2+. Scatchard plot analysis of the binding between 125I-PS and Mabs showed that the binding affinity of the antibodies ranged from 108 to 109 1/mol. Each EDTA-dependent Mab was then immobilized on Sepharose 4B-CNBr and used to purify PS from barium precipitation of citrated plasma. The fraction eluted with 2 mmol of CaCl2 from the immunoadsorbent appeared to contain only two proteins when stained with Cocmassie Blue. By immuno blotting, all Mabs reacted with both proteins, one comigrating with purified PS and the other with a MW >300.000. Essentially homogeneous PS, free from the high MW component, was obtained when the barium citrate adsorbate was applied to a DEAE-Sephadex column and the protein peack containing the balk of PS was sussequently applied to the immunoadsorbent and eluted with 2 mmol CaCl2.In summary, we have described an unusual set of EDTA-dependent monoclonal antibodies to PS and their use for the purification of homogeneous protein S from human plasma.
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8

Davies, T. A., D. Drotts, G. Weil, and E. R. Simons. "THROMBIN-INDUCED STIMULATION OF HUMAN PLATELETS LEADS TO AN INCREASE IN CYTOPLASMIC CALCIUM." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644471.

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Thrombin-induced stimulation of human platelets is accompanied by a dramatic increase in cytoplasmic calcium concentrations followed by a slow decrease. These changes are detected with indo 1. They are extremely rapid and are maximimal by 1015 seconds. Suspension studies, which reflect an average value over 3 × 107 cells/ml, indicate a thrombin dose-dependent increase in cytoplasmic calcium. However, flow cytometry indicates that subpopulations of cells are responding differently. The responses of these populations seem to be dependent on thrombin concentration. A maximal overall response is found when more than 50 % of the cells respond. This may explain multiple stimulations of the same suspension of cells at low thrombin dosesElevated extracellular Ca++ increases the maximal cytoplasmic response and significantly retards its subsequent decrease. When extracellular Ca++ is removed via addition of EGTA just before stimulation, the initial response is halved and the subsequent slow decrease is more marked and returns to lower (near-basal) levels. Intracellular Ca++ can be chelated with s - (0-am inophenoxy) - e thane-N, N, N',N'-tetraacet ic acid (BAPTA), which has a twofold greater affinity far Ca++ than does indo, but which does not fluoresce (at indo sensitive wavelengths) upon binding of Ca++. Cells loaded with both indo and BAPTA exhibit no rise in cytosolic Ca++ or altered membrane potential when stimulated with αthrombin, unlike cells loaded with indo alone. When Ca++ (2 mM) is added back to the extracellular buffer, these cells will take up the Ca++ at a constant rate as seen by a rise in indo fluorescence. When cytosolic Ca levels reach those of the resting platelets loaded with indo alone, these cells recover the αthrombin-indue ed Ca response of control platelets. However, they no longer depolarize partially under these same Ca++ replenished conditions. This implies that some of the Ca++ required for the platelet thrombin response comes from non-replenishable internal stores.
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9

Murayama, H., and N. U. Bang. "INCORPORATION OF PLASMINOGEN ACTIVATOR INHIBITOR INTO FIBRIN, AN ALTERNATIVE REGULATORY PATHWAY OF FIBRINOLYSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644442.

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A plasminogen activator inhibitor (PAI-1) Mj, 50 kd is normally found in plasma at low concentrations. Plasma levels increase sharply upon stimulation of endothelial cells with endotoxin or monokines and activated platelets secrete significant quantities of PAI-1. It is possible that high levels of PAI-1 may be achieved at the local sites of intravascular thrombi. Semipurified PAI-1 was therefore prepared from human platelets to study its affinity for fibrin (F). Approximately 50% PAI-1 adsorbed to F monomer immobilized on sepharose and desorbed under conditions of acidic pH and high ionic strength suggesting hydrogen bonding as the mode of interaction. Wells of 96-well microtiter plates were each coated with 50 yg [125I] plasminogen (P)-free fibrinogen and clotted with thrombin in the presence and absence of different concentrations of PAI-1. After extensive washing of the wells, they were incubated with 5 mU of tissue plasminogen activator (t-PA) and 5 mU of P for 6 h. Appropriate calibration curves utilizing different concentrations of t-PA and different concentrations of PAI-1 added to the supernatant rather than to F established that 8-15% of 21-166 mU PAI-1 incorporated into crosslinked (XL) F or noncrosslinked (NXL) F. Incorporated PAI strikingly inhibited fibrinolysis (FL). Percent inhibition of FL of XL or NXLF (Mean±S.D., N=5) plotted in the presence of 166, 83, 42 and 21 mU of PAI were: 83±3.3, 59.5±1.8, 29.7±5.2 and 15.2±6.14 for XLF and 78±5.3, 31±8.1, 14.5±10.5 and 0 Tor NXL F. As demonstrated by radioautography on SDS PAGE PAI-1 incorporated into F readily formed complexes with [125I] urokinase (u-PA). In these experiments, no evidence for crosslinking of PAI-1 into F has been obtained to date. In experiments utilizing agarose immobilized proteins, it was evident that not only F but also fibrinogen binds PAI-1; PAI-1 associated with F as well as fibrinogen is capable of forming complexes with [1251] u-PA.In contrast, fibronectin, collagen, gelatin and albumin did not bind PAI-1. Thus, PAI-1 in analogy with alpha-2 plasmin inhibitor may modulate physiological fibrinolysis through incorporation into fibrin.
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