Relevant bibliographies by topics / Immunoglobuline A

Contents

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

Academic literature on the topic 'Immunoglobuline A'

Author: Grafiati
Published: 4 June 2021
Last updated: 21 September 2024

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Journal articles on the topic "Immunoglobuline A"

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Puspitasari, Heni, Yuliana Praptiwi, and Lucia Suwanti. "Production and Characterization of Immunoglobuline Yolk as anti antigen membrane Toxoplasma gondii." Indonesian Journal of Tropical and Infectious Disease 6, no. 2 (December 29, 2016): 29. http://dx.doi.org/10.20473/ijtid.v6i2.1365.

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Toxoplasma gondii is an obligate parasite intracellular which can infected human and other mammalian. Immunoglobulin Y technology offers several advantages better than antibody production in mammals. This research was aimed to get immunoglobulin Y from egg yolk, to prove that antibody against membrane T. gondii antigen can produced from immunoglobulin Y and to know the characterization of immunoglobuline Y according to molecular weight by SDS PAGE and reactivation of antibody antigen by Western Blott. This research devided from many step : passase tachyzoites T. gondii into mice by peritoneal infection, cultivated the tachyzoite from intraperitoneal fluid, preparation of membrane antigen tachyzoite T. gondii, then immunization laying hens with membrane antigen, extraction and purification immunoglobuline Y from egg yolk and then protein analyzed by SDS PAGE and Western Blott. The result of this resarch showed that immunoglobulin Y from egg yolk can produced antibody against protein membrane T. gondii. The result of analyzed profile protein immunoglobuline Y according SDS PAGE has molecular weight 179,8 kDa. Analyzed from Western Blott showed that immunoglobulin Y can recognize antigen epitope of T. gondii on molecular weight 35,7 kDa and 78,8 kDa.
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Coulon, Séverine, Michaël Dussiot, Damien Grapton, Julien Rossignol, Thiago Trovati Maciel, Marc Benhamou, Renato C. Monteiro, Olivier Hermine, and Ivan C. Moura. "Immunoglobuline A1." médecine/sciences 28, no. 8-9 (August 2012): 692–95. http://dx.doi.org/10.1051/medsci/2012288006.

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Elhafidi, N., A. Asermouh, F. Benbrahim, and C. Mahraoui. "Le syndrome d’hyper-immunoglobuline E." Revue Française d'Allergologie 53, no. 3 (April 2013): 360. http://dx.doi.org/10.1016/j.reval.2013.02.086.

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Girodet, P. O., A. Casset, A. Magnan, F. de Blay, P. Chanez, and J. M. Tunon De Lara. "Immunoglobuline E et maladies respiratoires." Revue des Maladies Respiratoires 22, no. 6 (December 2005): 967–81. http://dx.doi.org/10.1016/s0761-8425(05)85728-6.

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Papo, T. "Immunoglobuline polivalenti per via endovenosa." EMC - AKOS - Trattato di Medicina 17, no. 3 (September 2015): 1–7. http://dx.doi.org/10.1016/s1634-7358(15)72345-4.

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Lapalus, Eva, and Alain Chevailler. "Diagnostic biologique d'une immunoglobuline monoclonale." Revue Française des Laboratoires 2000, no. 327 (November 2000): 67–74. http://dx.doi.org/10.1016/s0338-9898(00)80229-2.

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Papo, T. "Immunoglobuline polivalenti per via endovenosa." EMC - AKOS - Trattato di Medicina 26, no. 2 (June 2024): 1–6. http://dx.doi.org/10.1016/s1634-7358(24)49213-9.

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van der Does, E. "Intraveneus immunoglobuline bij secundairprogressieve multiple sclerose." Medisch-Farmaceutische Mededelingen 43, no. 1 (January 2005): 26. http://dx.doi.org/10.1007/bf03058530.

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Hello, M., S. Barbarot, A. Néel, J. M. Mussini, F. Jossic, B. Dupas, O. Espitias, A. Masseau, and M. Hamidou. "Placard cutané infiltré et immunoglobuline monoclonale." Annales de Dermatologie et de Vénéréologie 138, no. 12 (December 2011): A271—A272. http://dx.doi.org/10.1016/j.annder.2011.10.349.

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Brissaud, P., A. de Gramont, M. Krulik, and J. Debray. "Syndrome de Gougerot-Sjögren et immunoglobuline monoclonale." La Revue de Médecine Interne 6, no. 3 (June 1985): 331–32. http://dx.doi.org/10.1016/s0248-8663(85)80131-4.

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Dissertations / Theses on the topic "Immunoglobuline A"

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Malinge, Sophie. "Etude comparative des gènes Cmu et de leurs régions flanquantes chez le mouton et les mammifères." Poitiers, 1997. http://www.theses.fr/1997POIT2377.

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L'organisation generale des loci de chaines lourdes d'immunoglobulines est similaire chez tous les mammiferes : des genes v#h en nombre variable precedent en 5' des genes d (uniquement retrouves dans les chaines lourdes) presents en nombre plus restreint, eux memes precedant en 5' plusieurs segments j#h. Les genes des regions constantes (c#h) sont situes en 3' des genes j#h, ils determinent la classe de l'immunoglobuline. Ces loci contiennent aussi des regions de regulation de l'expression des ces genes. Chez le mouton, trois classes d'immunoglobulines ont ete caracterisees : 2 adnc c codant les formes secretees et membranaires de l'igm, 2 sous-classes d'igg (des segments c1 et c2) et l'ige (un segment c). Les travaux de recherches realises au cours de ma these ont consiste a analyser le locus igh du mouton. Le criblage d'une banque d'adn genomique de mouton, a l'aide de l'adnc c decrit au laboratoire, a permis d'isoler un clone contenant l'intron ovin dans lequel se trouvent des regions regulatrices. Nous avons decrit l'enhancer intronique qui regule l'expression des genes de chaines lourdes d'immunoglobulines. Il se trouve a 1 kb du dernier gene j#h et a 5 kb du gene c. Il contient tous les motifs caracteristiques des enhancers humain et murin et semble donc fonctionnel. L'intron j#h-c contient aussi la region switch s impliquee dans la commutation isotypique. Cette region s est egalement importante, car sans elle, les autres classes d'immunoglobulines ne seraient pas exprimees. La composition de la region s ovine, sa taille et sa localisation sur le genome sont similaires a ce qui est decrit chez d'autres mammiferes. Cette region intervient donc probablement dans la commutation des genes c#h ovins. La sequence entiere du gene c ainsi que ses exons de membrane sont presents dans ce clone : nous avons decrit l'organisation genomique du gene c ovin. L'analyse des sequences montre que ce gene peut etre exprime. La recherche du gene c ovin (localise en 3' du gene c chez les primates et les rongeurs) a ete realisee par une marche sur le chromosome. L'analyse de la portion du genome ovin s'etendant sur 15 kb en aval des exons de membrane (et qui devrait normalement contenir le gene c) a ete realisee : aucune trace de gene c n'a ete trouvee. Des recherches de ce gene par pcr et par southern blots se sont revelees negatives. Nous avons ainsi apporte des arguments en faveur de l'absence d'un gene c chez le mouton.
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Das, Mrinmoy. "The regulatory effects of circulating normal immunoglobulins on autophagy and Th17 response." Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066153/document.

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Les immunoglobulines circulantes jouent un rôle critique dans l’homéostasie immune en modulant les fonctions des cellules du système immunitaire. Au cours de ma thèse, j’ai exploré les effets régulateurs des immunoglobulines G thérapeutiques (IVIG) et des immunoglobulines A monomériques circulantes (mIgA) sur l’autophagie et les réponses Th17 respectivement. Les IVIg sont une préparation thérapeutique d’IgG normales poolées. Elles ont utilisées comme agent anti-inflammatoire dans le traitement de maladies auto-immunes et inflammatoires variées. Cependant, les mécanismes ne sont pas complètement élucidés et plusieurs mécanismes mutuels et non exclusifs ont été proposés. L’autophagie est un important processus biologique impliquant la dégradation lysosomale des composants cellulaires endommagés et des protéines mal repliées. Il y a plusieurs preuves montrant l’implication de l’autophagie dans les maladies auto-immunes et auto-inflammatoires incluant la découverte de polymorphismes dans des gènes liés à l’autophagie. J’ai montré que l’induction de l’autophagie par les IVIG représente un nouveau mécanisme d’action permettant leur effet thérapeutique dans les maladies auto-immunes et inflammatoires. Les Th17 représentent une cible attractive pour traiter plusieurs maladies inflammatoires et auto-immunes. Malgré le fait qu’elles sont le deuxième anticorps le plus abondant dans la circulation, la function immunorégulatrice des IgA n’est relativement pas explorée. J’ai montré que les IgA monomériques (mIgA) inhibent la différentiation et l’amplification des cellules Th17 humaines et la production de leur cytokine effectrice IL-17A
Circulating immunoglobulins play a critical role in the immune homeostasis by modulating the functions of immune cells. In my thesis, I investigated the regulatory effects of therapeutic immunoglobulin G (IVIG) and circulating monomeric immunoglobulin A (mIgA) on autophagy and human Th17 response respectively. IVIG is a therapeutic preparation of pooled normal IgG. It is used as an anti-inflammatory agent in the treatment of a wide variety of autoimmune and inflammatory diseases. However, the mechanisms are not yet fully elucidated and several mutually non-exclusive mechanisms have been proposed. Autophagy is an important biological process involving lysosomal degradation of damaged cellular components and misfolded proteins. There are several evidences that support the involvement of autophagy in autoimmune and auto- inflammatory disorders including the discovery of polymorphisms in autophagy-related genes. I show that induction of autophagy by IVIG represents a novel mechanism of action in achieving therapeutic effect in autoimmune and inflammatory diseases. Th17 cells represent an attractive target to treat several inflammatory and autoimmune diseases. Despite being second most abundant antibody in the circulation, the immunoregulatory function of IgA is relatively unexplored. I have shown that monomeric IgA (mIgA) inhibits differentiation and amplification of human Th17 cells and the production of their effector cytokine IL-17A
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Martinez-Rivas, Gemma. "Exploration des mécanismes physiopathologiques de l'amylose et évaluation des nouvelles approches thérapeutiques." Electronic Thesis or Diss., Limoges, 2024. http://www.theses.fr/2024LIMO0052.

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L’amylose à chaînes légères (AL) est l’une des formes les plus courantes d’amylose systémique, provoquée par le dépôt de chaînes légères (LC) d’immunoglobulines (Ig) sous forme de fibrilles amyloïdes dans les tissus, entraînant une dysfonction organique. Les formes les plus fréquentes et sévères affectent les reins et le cœur, cette dernière étant associée à un mauvais pronostic. Malgré des efforts considérables pour comprendre les mécanismes de formation des fibrilles et leur toxicité, l’absence de modèles in vivo fiables entrave l’étude de la maladie dans son contexte physiologique. Cette thèse s’intéresse à l’exploration des mécanismes physiopathologiques dans l’amylose AL. Pour cette étude, nous avons mis en place un modèle murin reproduisant la pathologie humaine. Sous induction, notre modèle développe des atteintes cardiaques, associées à une dysfonction de l’organe, qui peut être assimilée aux effets observés dans les patients. Ainsi, la caractérisation de ce modèle a montré sa pertinence à reproduire la physiopathologie humaine. Ce modèle, unique au monde, ouvre des portes à l’exploration des mécanismes d’agrégation et de dépôt des chaînes légères, mais peut constituer également un outil pour des tests thérapeutiques et de diagnostic
Light chain (AL) amyloidosis is one of the most common forms of systemic amyloidosis, caused by the deposition of immunoglobulin (Ig) light chains (LC) in the form of amyloid fibrils in tissues, leading to organ dysfunction. The most frequent and severe forms affect the kidneys and heart, with the latter associated with a poor prognosis. Despite considerable efforts to understand the mechanisms of fibril formation and their toxicity, the lack of reliable in vivo models hinders the study of the disease in its physiological context. This thesis focuses on exploring the pathophysiological mechanisms in AL amyloidosis. For this study, we developed a mouse model that reproduces the human pathology. Under induction, our model develops cardiac involvement associated with organ dysfunction, which can be compared to the effects observed in patients. Thus, the characterization of this model has shown its relevance in reproducing human pathophysiology. This unique model opens new avenues for exploring the mechanisms of light chain aggregation and deposition, and can also serve as a tool for therapeutic and diagnostic testing
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Carpenet, Guéry Hélène. "Radiomarquage au 99mTc des IgA et IgG : optimisation du marquage, étude in vitro, biodistribution chez l'animal sain et sur modèle tumoral." Thesis, Limoges, 2015. http://www.theses.fr/2015LIMO0074/document.

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Depuis leur découverte en 1975 par Köhler et Milstein, le monde des Ac monoclonaux a beaucoup évolué. Ils occupent actuellement une place prépondérante dans la prise en charge de nombreux cancers. De nos jours, les Ac monoclonaux, ayant une AMM ou en essai clinique, sont tous de classe IgG voire IgG1. Cette classe d’Ac a cependant montré des limites à son utilisation, et l’étude d’autres isotypes d’Ac, comme les IgA, pourrait être intéressante. Les IgA, isotype d’Ac particulier en raison notamment de leur hétérogénéité dans les formes moléculaires, demeurent peu étudiées à l’instar des IgG. Dans ce travail, nous proposons un radiomarquage des IgA monomériques, polymériques et sécrétoires, avec le 99mTc par une méthode indirecte impliquant le 2-iminothiolane et le cœur tricarbonyl. Par le biais de ce radiomarquage, la biodistribution des IgA monomériques et polymériques après administration i.v. a été évaluée chez l’animal sain et chez l’animal porteur de tumeur à localisation muqueuse. Ces études nous ont permis d’entrevoir le potentiel diagnostique des IgA, mais aussi leur intérêt en thérapie ciblée de tumeurs à localisation muqueuse. D’autre part, grâce à leur résistance enzymatique et au phénomène de retranscytose, une nouvelle voie d’administration des Ac monoclonaux pourrait être développée. Dans cette optique, des IgA sécrétoires ont été administrées par voie orale lors d’études préliminaires de biodistribution
Since their discovery in 1975, by Köhler and Milstein, monoclonal antibodies (mAbs) world has significantly evolved and they currently hold a prominent place in cancers care. Today, the mAbs, having a marketing authorization or in clinical trial, are all IgG class (IgG1). However, this Ab class showed limitations on its use, and the study of other isotypes, such as IgA, could be interesting. Unlike IgG, IgA, original isotype particularly because of their heterogeneity in molecular forms, remains understudied. In this work, we propose a radiolabeling of monomeric, polymeric and secretory IgA with 99mTc by an indirect method, involving 2-iminothiolane and tricarbonyl core. Biodistribution of radiolabeled monomeric and polymeric IgA was evaluated, after intravenous administration, in healthy animals and in mucosal tumor-bearing animals. These studies have allowed us to glimpse the IgA diagnostic potential, but also their interest in targeted therapy of tumors with mucosal localization. Moreover, thanks to their enzymatic strength and retranscytosis, a new administration route of mAbs could be developed. In this context, secretory IgA were administered orally in preliminary biodistribution studies
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Nourichafi, Nadia. "Purification des immunoglobulines plasmatiques humaines par chromatographie à partir de la fraction II+III de Cohn." Nancy 1, 1993. http://www.theses.fr/1993NAN19429.

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Audhuy, Stéphane. "Développement et automatisation de coffrets de détection d'immunoglobulines G et M toxoplasmiques." Université Louis Pasteur (Strasbourg) (1971-2008), 1996. http://www.theses.fr/1996STR13292.

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Alcaraz, Gisèle. "Etudes structurales d'une immunoglobuline D de myélome de rat et du Fc-récepteur pour l'IgE exprimé par les mastocytes et les basophiles." Aix-Marseille 2, 1987. http://www.theses.fr/1987AIX22044.

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L'etude biochimique d'une igd de myelome de rat a permis de mettre en evidence la structure particuliere de cet isotype, le domaine c delta 2 present chez l'homme est absent. Cette perte d'un domaine n'affecte pas dans ces especes (rat, souris) la propriete d'extreme sensibilite au clivage dans la region charniere qui caracterise l'igd. La fonction de cet isotype est encore inconnue, bien que plusieurs modeles lui attribuent un role dans la regulation de la reponse anticorps, comme le fait qu'il s'agisse, avec l'igm, d'un des recepteurs immunoglobuliniques majeurs de lymphocyte b. Le fc-recepteur pour l'ige est exprime sur les mastocytes et les basophiles, il declenche de l'activation cellulaire conduisant aux manifestations allergiques, c'est une proteine multimerique (mise au point d'une methode de purification preparative)
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Billard, Florence. "Utilisation des immunoglobulines polyvalentes dans le traitement du Purpura thrombopénique idiopathique." Paris 5, 1989. http://www.theses.fr/1989PA05P029.

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Martin, Charlotte Morin-Niglais Odile. "Sérologie de la toxoplasmose." [S.l.] : [s.n.], 2004. http://theses.univ-nantes.fr/thesemed/PHmartinc.pdf.

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Akram, Kasmi. "Mise au point d'une technique immuno-enzymatique (ELISA) appliquée au titrage des facteurs rhumatoïdes : Ig. M, Ig. G, et Ig. A." Lyon 1, 1985. http://www.theses.fr/1985LYO1W234.

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Books on the topic "Immunoglobuline A"

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1942-, Honjo T., Alt Frederick W, and Rabbitts T. H, eds. Immunoglobulin genes. London: Academic Press, 1989.

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Slayton, Kaetzel Charlotte, ed. Mucosal immune defense: Immunoglobulin A. New York: Springer, 2007.

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Slayton, Kaetzel Charlotte, ed. Mucosal immune defense: Immunoglobulin A. New York: Springer, 2007.

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C, Howard Gary, and Bethell Delia R, eds. Basic methods in antibody production and characterization. Boca Raton: CRC Press, 2001.

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Kaushik, Azad K., and Yfke Pasman. Comparative immunoglobulin genetics. Toronto: Apple Academic Press, 2014.

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Paolo, Casali, Silberstein Leslie E, and New York Academy of Sciences., eds. Immunoglobulin gene expression in development and disease. New York: New York Academy of Sciences, 1995.

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Slayton, Kaetzel Charlotte, ed. Mucosal immune defense: Immunoglobulin A. New York: Springer, 2007.

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Lazarus, Alan H. Immunoglobulin therapy. Bethesda, Md: AABB Press, 2010.

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John, Stewart. The primordial VRM system and the evolution of vertebrate immunity. Austin: R.G. Landes, 1994.

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Donata, Vercelli, ed. IgE regulation: Molecular mechanisms. Chichester: J. Wiley, 1997.

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Book chapters on the topic "Immunoglobuline A"

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Wenger, F. A., C. A. Jacobi, H. Zuckermann, H. D. Volk, and J. M. Müller. "Intravenöse Therapie mit 7S-Immunoglobuline bei durch Sepsis bedingter Immunparalyse. Eine prospektive Beobachtungsstudie." In Bilanz zur Jahrtausendwende, 876–78. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-60248-1_199.

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Bot, Adrian, and Dan Smith. "Fc Receptor Targeting With Recombinant Immunoglobulins and Immunoglobulin Formulations." In Cellular Drug Delivery, 287–310. Totowa, NJ: Humana Press, 2004. http://dx.doi.org/10.1007/978-1-59259-745-1_16.

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Gupta, Anil. "Immunoglobulins." In Comprehensive Biochemistry for Dentistry, 585–91. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-1035-5_23.

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Long, Joanna. "Immunoglobulins." In Encyclopedia of Behavioral Medicine, 1150–51. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-39903-0_465.

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Boltz, Marie, Holly Rau, Paula Williams, Holly Rau, Paula Williams, Jane Upton, Jos A. Bosch, et al. "Immunoglobulins." In Encyclopedia of Behavioral Medicine, 1039–41. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-1005-9_465.

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Ward, Tony Milford. "Immunoglobulins." In Proteins and Tumour Markers May 1995, 1217–47. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0681-8_42.

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Long, Joanna. "Immunoglobulins." In Encyclopedia of Behavioral Medicine, 1–2. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6439-6_465-2.

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van Balen, J. A. M., A. A. Demeulemeester, M. Frölich, K. Mohrmann, L. M. Harms, W. C. H. van Helden, L. J. Mostert, and J. H. M. Souverijn. "Immunoglobulinen." In Memoboek, 141. Houten: Bohn Stafleu van Loghum, 2012. http://dx.doi.org/10.1007/978-90-313-9129-5_77.

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Felippe, Julia B. "Immunoglobulins." In Interpretation of Equine Laboratory Diagnostics, 273–81. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781118922798.ch46.

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Barisani-Asenbauer, Talin. "Immunoglobulins." In Intraocular Inflammation, 339–43. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-540-75387-2_26.

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Conference papers on the topic "Immunoglobuline A"

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Nabok, Alexei V., Nickolaj F. Starodub, Asim K. Ray, and Aseel K. Hassan. "Registration of immunoglobuline AB/AG reaction with planar polarization interferometer." In Environmental and Industrial Sensing, edited by Robert A. Lieberman. SPIE, 2000. http://dx.doi.org/10.1117/12.411710.

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Dichtelmuller, H., and W. Stephan. "IN VIVO AND IN VITRO NEUTRALIZATION OF BACTERIAL TOXINES BY IGM ENRICHED AND CONVENTIONAL I. V. IMMUNOGLOBULINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644255.

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Severe septic phenomena are caused bybacterial toxins. We therefore investigated the neutralization of toxins derived from Staphylococcus aureus and Pseudcmonas aeruginosa by different i.v. irtmunoglobulin preparations using hemolysis inhibition tests and mouse protection tests. The efficacy of conventional i.v. immunoglobulin containing preparations were compared with an IgM enriched i.v. immunoglobulin (Pentaglobin).For hemolysis inhibition tests sterile filtered supernatant of Staphylococcusaureus was prepared and given to human erythrocytes. When IgM enriched immunoglobulin was added, toxin depended hemolysis was inhibited. By addition of three different i.v. immunoglobulin preparationsno inhibition of hemolysis was observed. In order to confirm these results in vivo, mice were exposed to the toxic supernatant of Staphylococcus aureus intraperitoneally and treated with i.v. immunoglobulins (3.1 mg/animal) 30 min after toxin exposure. Significant protection of toxin exposed animals was achieved by IgM enriched i.v. immunoglobulin (92 % protection) but not by conventional i.v. immunoglobulin (17 % protection). Similar results were obtained when mice were exposed to toxic supernatant of Pseudcmonas aeruginosa instead of Staphylococcus aureus. We therefore conclude, that IgM is essential for neutralization of bacterial toxins and IgM enriched i.v. immunoglobulins are more effective in therapy of severe septic phenomena, compared to conventional i.v. immunoglobulins.
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"Statistical relations between N-glycome of circulating immunoglobuline G and total plasma N-Glycome." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-010.

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Köhler-Vajita, K., L. Grütler, and F. Bidlingmaier. "Immunoglobulins of HIV positive and negative haemophiliac children treated with different concentrates." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644138.

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Aim of this investigation is the quantitative comparison of theimmunoglobulins G, A, M in haemophiliac children treated with different types of factor VIII concentrates.Patients and methodsSince May 1984 22 patients with haemophiliaA were investigated. Instead of the more often analysed parameterof the cellular immunity now we want to draw the attention to the immunoglobuline values, especiallyof the HIV negative group of patients treated exclusively with Haemate HS Behringwerke in comparison with other differently treated HIV positive and negative patients.Results The group of patients treated exclusively with Haemate HS Behringwerke (in solution heatsterilized) shows completely normal immunolobuline levels and a safe HIV negativity.Patients treated with conventional, later with heat treated (inlyophilized form) concentrates can be divided into HIV positive and negative groups. HIV positive heamophiliacs show pathological IgG and border line IgA and IgM values. HIV negative patients have IgG, A levels within the normal limits -but clearly higher than the Haemate group. A correlation withliver enzyme status (hepatitis B, NANB) could not be found.
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Toti, F., A. Stierlé, M. L. Wiesel, A. Schwartz, J. M. Freyssinet, and J. P. Cazenave. "PRODUCTION OF ANTIBODIES TO HUMAN VON WILLEBRAND FACTOR IN LAYING HENS. ISOLATION OF IMMUNOGLOBULINS AND APPLICATIONS TO THE DETECTION OF MOLECULAR DEFECTS OF VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644084.

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Von Willebrand disease (vWD) is an inherited disorder of primary hemostasis caused by deficiency or structural abnormalities of von Willebrand factor (vWF). VWF circulates in plasma and is also present in platelets. Plasma vWF, the carrier protein for factor VIII, is a large multimeric glycoprotein composed of identical subunits linked by disulfide bridges. Plasma and platelet vWF display distinct multimeric electrophoretic patterns. The different vWD subtypes can be classified either by the determination of vWFantigen (vWFíAg) and/or by multimer distribution. Antibodies to human vWF were raised in laying hens by intramuscular injections of purified human vWF. Immunoglobulins were isolated from egg yolks by selective polyethylene glycol and ammonium sulfate precipitations. These antibodies appeared to be monospecific, as they did not react with the plasma proteins of a patient with severe vWD. The pullets received weekly 50 μg vWF for 4 weeks and then had monthly injections. The antibodies occurred as early as the third injection, the yield being 300 to 500 mg of immunoglobulin per week (6-7 eggs). The titre could be constant over periods greater than 1 year. These immunoglobulins to vWF were tested in vWFíAg electroimmunoassays and for the multimer analysis of plasma and platelet vWF by electrophoresis and immunoblotting techniques. In no case could a difference be detected between assays performed with rabbit monospecific antiserum or with yolk immunoglobulins to human vWF. Ten to 12 multimers could be revealed for normal plasma vWF and up to 12 to 14 bands for normal platelet vWF (1.7% agarose). In the case of vWD, the electrophoresis patterns were identical with both antibodies. Thus, antibodies to vWF raised in laying hens are a suitable tool to detect and to characterize vWD. Although they do not interact with protein A, yolk antibodies are certainly advantageous to produce, as they do not contain IgM or IgA. Immunoglobulin fractions can contain up to 10 % of specific antibodies. Since they are available in larger quantities and are easy to isolate, larger homogeneous batches of antibodies can be obtained. This method may easily be applied to develop antibodies to a variety of antigens.
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Krasnoshtanova, Alla, and Alesya Yudina. "PRODUCTION OF ANTIBODIES FROM POULTRY YOLK (IgY) AND INVESTIGATION OF THEIR IMMUNOCHEMICAL PROPERTIES." In GEOLINKS Conference Proceedings. Saima Consult Ltd, 2021. http://dx.doi.org/10.32008/geolinks2021/b1/v3/17.

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"A particularly important aspect of immunology is to develop non-invasive methods of obtaining antibodies which could be a great alternative to traditional ones that based on the harmful procedure of isolation of immunoglobulins from animal blood sera. That’s why the extraction of antibodies from poultry egg yolks (IgY) is the most promising. Due to the fact of variation of IgY structural features that determine the definite immunochemical properties, yolk antibodies in comparison with mammalian immunoglobulins (IgG) does not interact with rheumatoid factor (Rf), contribute to the activation of the complement system, bind to the Fc-receptor (FcR), and also has weak cross-reactivity, which confirms the possibility of their widespread use in medicine and food. Also the presence of phylogenetic distance between chickens and mammalians guarantees immune response against conservative mammalian protein molecules which is highly important for the creation of new generation test systems. The aim of this work is to develop a selective method of producing high-purity immunoglobulin Y preparations from the yolk of chicken eggs. There were adopted selective conditions of isolation of IgY under spontaneous thawing procedure at the room temperature of firstly frozen yolk solution in a sodium-phosphate buffer mixed with water (pH 5.0) in a ratio of 1:6, which leads to receiving a water-soluble fraction further precipitated with the sodium chloride at a concentration of 10% of the solution mass and subsequently concentrated using ultrafiltration with membrane UAM-10, that allows achieving the content of IgY not less than 95% per dry substance in immunoglobulin fraction. It is possible to produce a protein fraction with a protein content of at least 9 g/l. The purity of the immunoglobulin fraction was verified using polyacrylamide gel electrophoresis. The presence of a light chain in the IgY solution was proved to be a low-molecular compound using the method of gel-filtration-chromatography. The immunological activity of IgY was studied with respect to bovine serum albumin (BSA) as an antigen. The enzymatic resistance of IgY against proteolytic enzymes was tested in area of the gastrointestinal tract."
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Bushueva, T. V., N. A. Roslaya, and E. P. Karpova. "IMMUNOLOGICAL FACTORS OF STREPTOCOCCUS PNEUMONIAE PERSISTENCE IN WORKERS OF COPPER SMELTER." In The 17th «OCCUPATION and HEALTH» Russian National Congress with International Participation (OHRNC-2023). FSBSI «IRIOH», 2023. http://dx.doi.org/10.31089/978-5-6042929-1-4-2023-1-96-100.

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In article we touch upon the problem of immunological factors of persistence of Streptococcus pneumoniae in employees of the copper electrolytic refining enterprise. Materials and methods. A survey of 100 employees of the enterprise for the electrolytic refining of copper was carried out. The main group — 50 smelters of the anode section of the copper smelter, the control group — 50 engineering and technical workers. Smears were taken from the posterior pharyngeal wall to detect S. pneumoniae DNA. Immunological examination included the determination of cellular immunity by flow cytometry, humoral immunity with the determination of immunoglobulins by ELISA. Secretory immunoglobulin A (SigA) was determined in the oral fluid. Results and conclusions. S. pneumoniae was more often found in workers of the main group (p<0.05). Smoking tobacco products increases the chance of developing S. pneumoniae carriage. In workers of the main group, suppression of humoral factors of immunity was revealed; with S. pneumoniae+, the relative number of T‑helpers is reduced and the bactericidal activity of neutrophils is enhanced.
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Vinazzer, H., and U. Pangraz. "HEPARIN COFACTOR II: A SIMPLE ASSAY METHOD." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644349.

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A photometric assay method for heparin cofactor II (HC II) is described. In a first step antithrombin III (AT III) in plasma is blocked by an anti human AT III immunoglobuline from goats. After dilution of this plasma with Tris buffer pH 8.4 containing 3 IU/ml heparin and addition of thrombin the remaining thrombin activity is measured by use of the chromogenic substrate S-2238 Kabi. The following preliminary experiments were carried out: Variation of the amount of anti-AT III added to plasma resulted in complete inactivation of 1.25 units AT III by 1.0 ml of the inhibitor. Incubation of 1 ml anti AT III with 1 ml purified AT III ( 1 U/ml} or with 1 ml normal plasma completely abolished AT III activity within 60 sec. Incubation of the reaction mixture with thrombin resulted in maximum inactivation after 180 sec. This is in contrast to AT III activated by heparin which immediately inactivates thrombin. Anti-Xa activity after depletion of AT III was assayed in a similar way by addition of factor Xa to the reaction mixture and measuring the remaining Xa activity by the substrate S-2222. In these tests no anti Xa-activity was found after AT III depletion. From these experiments there was assumed that the anti thrombin activity measured under the following conditions was due to the action of HC II:Plasma ( 50 μl) was mixed with anti AT III (50 μl) and was incubated for 60 sec. Tris buffer with heparin pH 8.4 (900 μl) was added. From this mixture 200 μl was pipetted into a cuvette at 37°C followed by 200 μl thrombin ( 2 IU/ml). After an incubation time of 180 sec 200 μl S-2238 ( 2 mmol/1) was added and the difference in OD/min was determined at 405 nm. A calibration curve was made by series of dilutions of normal AT III depleted plasma from 20 healthy individuals. The following preliminary results ofrHC II activity as a percentage were obtained:
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Li, J., and Z. Zhang. "AB1033 The expression of immunoglobulin g and immunoglobulin g4 in lymphoma." In Annual European Congress of Rheumatology, 14–17 June, 2017. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2017-eular.3999.

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Jørgensen, M. "HEPARIN INDEPENDENT PURIFICATION OF ANTITHROMBIN III (AT III) BY IMMUNO-AFFINITY CHROMATOGRAPHY RESULTING IN A FUNCTIONALLY INTACT MOLECULE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643682.

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Previous methods for purification of AT III are based on its heparin-binding capacity. However, in congenital AT III deficiency abnormal inhibitor molecules with impaired binding of heparin and/or thrombin has been reported. The aim of the present study was to develop a purification method based on immuno-affinity chromatography, and thus independent of the heparin binding capacity.Rabbits were immunized with human AT III purified by a three-step procedure involving dextran sulphate precipitation, affinity chromatography on heparin-Sepharose and ion-exchange chromatography on DEAE-Sephadex A-50. Rabbit immunoglobulins against human AT III were isolated by affinity chromatography using purified human AT III coupled to CNBr-activated Sepharose 4B. Trace amounts of immunoglobulin against human albumin, IgG and IgM were removed by solid phase immunoadsorption. The highly purified immunoglobulins against human AT III were coupled to CNBr-activated Sepharose 4B. This anti-AT III-Sepharose was used for single-step purification of AT III from plasma. Elution was performed by Na-citrate buffer at pH 3.0 and the eluted fractions immediately neutralized. The recovery was more than 60%.The purified AT III appeared as a single protein band in SDS-poly-acrylamide gel electrophoresis with or without reduction. Affinity purified AT III and AT III purified by the three-step procedure were indistinguishable when analyzed by crossed immunoelectrophoresis in the absence and the presence of heparin isoelectrical focusing in polyacrylamid gel at a pH 4-6.5 gradient, and SDS-polyacrylamide gel electrophoresis. AT III antigen concentration was determined by electroimmunoassay and the reactive site concentration determined by titration with purified human thrombin using Phe-Pip-Arg-Nan (S-2238) as substrate. The ratio (active site conc.)/(antigen conc.) was identical in the two AT III preparations. It is concluded that this single-step immuno-affinity chromatography gives a high recovery from plasma of a highly purified functionally intact AT III molecule. The purification method is independent of the heparin binding capacity of AT III. This is of particular importance for the purification and characterization of abnormal AT III molecules with impaired heparin-binding site.
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Reports on the topic "Immunoglobuline A"

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Steplewski, Z., P. Curtis, J. Hainfeld, L. Mausner, R. Mease, and S. Srivastava. Selection and manipulation of immunoglobulins for radionuclide delivery. Office of Scientific and Technical Information (OSTI), December 1992. http://dx.doi.org/10.2172/10139566.

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Hammer, Carrie, Howard Tyler, James A. Roth, and James D. Quigley. Characterization of Reactions to Intravenous Immunoglobulin in Neonatal Calves. Ames (Iowa): Iowa State University, January 2004. http://dx.doi.org/10.31274/ans_air-180814-837.

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Kenney, James J. Transfection of Murine and Human Hematopoietic Progenitors with Rearranged Immunoglobulin Genes,. Fort Belvoir, VA: Defense Technical Information Center, July 1992. http://dx.doi.org/10.21236/ada253974.

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Kenny, James J. Transfection of Murine and Human Hematopoietic Progenitors with Rearranged Immunoglobulin Genes. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada243424.

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Kenny, James J. Transfection of Murine and Human Hematopoietic Progenitors with Rearranged Immunoglobulin Genes. Fort Belvoir, VA: Defense Technical Information Center, February 1992. http://dx.doi.org/10.21236/ada245750.

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Block, Timothy M., Songming Chen, Anand S. Mehta, and Terry J. Henderson. A Glycoform of Immunoglobulin G (IgG) as an Early Biomarker of Exposure to Nonhuman Substances. Fort Belvoir, VA: Defense Technical Information Center, December 2012. http://dx.doi.org/10.21236/ada570851.

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Fu, Chengcheng, Xiaohong Wang, Bin Wang, Lingjie Xu, and Wenming Chen. The clinical characteristics of immunoglobulin light chain amyloidosis in Chinese population: A systematic scoping review. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, September 2021. http://dx.doi.org/10.37766/inplasy2021.9.0086.

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Middlebrooks, Bobby L. Investigation of the Role of Immunoglobulin Classes and Subclasses in Humoral and Mucosal Immunity in Cetaceans. Fort Belvoir, VA: Defense Technical Information Center, June 2005. http://dx.doi.org/10.21236/ada452454.

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Mackey, Katherine, Irina Arkhipova-Jenkins, Charlotte Armstrong, Emily Gean, Johanna Anderson, Robin A. Paynter, and Mark Helfand. Antibody Response Following SARS-CoV-2 Infection and Implications for Immunity: A Rapid Living Review. Agency for Healthcare Research and Quality (AHRQ), March 2021. http://dx.doi.org/10.23970/ahrqepccovidimmunity.

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 Evidence suggests that the majority of adults develop detectable levels of immunoglobulin M (IgM) and immunoglobulin G (IgG) antibodies following infection with SARS-CoV-2 (moderate strength of evidence* [SoE]).  IgM levels peak approximately 20 days after symptom onset or RT-PCR diagnosis and subsequently decline. IgG levels peak approximately 25 days after symptom onset or RT-PCR diagnosis and may remain detectable for at least 120 days (moderate SoE*).  Almost all adults develop neutralizing antibodies in response to SARS-CoV-2 infection, and these antibodies may remain detectable for at least 152 days (low SoE*).  A small percentage of people do not develop antibodies in response to SARS-CoV-2 infection for reasons that are largely unclear but may be related to less severe disease or absence of symptoms.  Antibody prevalence does not appear to vary by age or sex, but older age may be associated with higher antibody levels (low SoE*). Non-White race may be associated with higher antibody prevalence and levels (low SoE*). COVID-19 severity and presence of symptoms may also be associated with higher antibody prevalence or levels (low SoE*). More evidence is needed to draw stronger conclusions regarding how the antibody response varies by patient characteristics and disease factors.  Studies to date have not established the relationship between the development of antibodies after RT-PCR-diagnosed SARS-CoV-2 infection and the risk of reinfection. Studies based on index serologic testing suggest that the presence of antibodies is associated with a lower risk of a subsequent positive SARS-CoV-2 RT-PCR test.
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Varbanova, Viktoria, Snejina Mihailova, Elissaveta Naumova, and Anastasiya Mihaylova. Distribution of Killer-cell Immunoglobulin-like Receptors (KIR) and their HLA Class I Ligands in the Bulgarian Population. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, July 2020. http://dx.doi.org/10.7546/crabs.2020.07.14.

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