Letteratura scientifica selezionata sul tema "Immunoglobulin A"

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Articoli di riviste sul tema "Immunoglobulin A"

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Hasegawa, Haruki. "Aggregates, Crystals, Gels, and Amyloids: Intracellular and Extracellular Phenotypes at the Crossroads of Immunoglobulin Physicochemical Property and Cell Physiology". International Journal of Cell Biology 2013 (2013): 1–22. http://dx.doi.org/10.1155/2013/604867.

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Recombinant immunoglobulins comprise an important class of human therapeutics. Although specific immunoglobulins can be purposefully raised against desired antigen targets by various methods, identifying an immunoglobulin clone that simultaneously possesses potent therapeutic activities and desirable manufacturing-related attributes often turns out to be challenging. The variable domains of individual immunoglobulins primarily define the unique antigen specificities and binding affinities inherent to each clone. The primary sequence of the variable domains also specifies the unique physicochemical properties that modulate various aspects of individual immunoglobulin life cycle, starting from the biosynthetic steps in the endoplasmic reticulum, secretory pathway trafficking, secretion, and the fate in the extracellular space and in the endosome-lysosome system. Because of the diverse repertoire of immunoglobulin physicochemical properties, some immunoglobulin clones’ intrinsic properties may manifest as intriguing cellular phenotypes, unusual solution behaviors, and serious pathologic outcomes that are of scientific and clinical importance. To gain renewed insights into identifying manufacturable therapeutic antibodies, this paper catalogs important intracellular and extracellular phenotypes induced by various subsets of immunoglobulin clones occupying different niches of diverse physicochemical repertoire space. Both intrinsic and extrinsic factors that make certain immunoglobulin clones desirable or undesirable for large-scale manufacturing and therapeutic use are summarized.
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Gong, Yuxin, Bo Liao, Dejun Peng e Quan Zou. "Accurate Prediction and Key Feature Recognition of Immunoglobulin". Applied Sciences 11, n. 15 (27 luglio 2021): 6894. http://dx.doi.org/10.3390/app11156894.

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Immunoglobulin, which is also called an antibody, is a type of serum protein produced by B cells that can specifically bind to the corresponding antigen. Immunoglobulin is closely related to many diseases and plays a key role in medical and biological circles. Therefore, the use of effective methods to improve the accuracy of immunoglobulin classification is of great significance for disease research. In this paper, the CC–PSSM and monoTriKGap methods were selected to extract the immunoglobulin features, MRMD1.0 and MRMD2.0 were used to reduce the feature dimension, and the effect of discriminating the two–dimensional key features identified by the single dimension reduction method from the mixed two–dimensional key features was used to distinguish the immunoglobulins. The data results indicated that monoTrikGap (k = 1) can accurately predict 99.5614% of immunoglobulins under 5-fold cross–validation. In addition, CC–PSSM is the best method for identifying mixed two–dimensional key features and can distinguish 92.1053% of immunoglobulins. The above proves that the method used in this paper is reliable for predicting immunoglobulin and identifying key features.
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Tsavaris, N., D. Tsigalacis, C. Kosmas, CH Koufos, G. Vaiopoulos, M. Tzivras, G. Kouraklis et al. "Preliminary Evaluation of the Potential Prognostic Value of Serum Levels of Immunoglobulins (IgA, IgM, IgG, IgE) in Patients with Gastric Cancer". International Journal of Biological Markers 13, n. 2 (aprile 1998): 87–91. http://dx.doi.org/10.1177/172460089801300204.

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Sixty patients with advanced gastric carcinoma who refused to receive cytotoxic chemotherapy were examined for serum immunoglobulin levels (IgG, IgM, IgA, IgE). Three samples were obtained every two months thereafter. The group of patients who had above-normal values of one or more of the examined immunoglobulins had a longer survival than the other (p<0.024). Immunoglobulin values were independent of the Helicobacter pylori antibody titer and of acute phase reactants. It is concluded that survival potentially correlates with serum immunoglobulin levels. Further studies including larger numbers of patients and correlating serum immunoglobulin levels with specific clinical parameters are needed to establish the prognostic role of serum immunoglobulins in patients with gastric carcinoma.
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Puspitasari, Heni, Yuliana Praptiwi e Lucia Suwanti. "Production and Characterization of Immunoglobuline Yolk as anti antigen membrane Toxoplasma gondii". Indonesian Journal of Tropical and Infectious Disease 6, n. 2 (29 dicembre 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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Srikumaran, S., E. A. Kluever, D. V. Onisk e K. Hariharan. "Quantitation of bovine immunoglobulins in culture fluids by use of sandwich radioimmunoassay with monoclonal antibodies". American Journal of Veterinary Research 52, n. 2 (1 febbraio 1991): 243–46. http://dx.doi.org/10.2460/ajvr.1991.52.02.243.

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SUMMARY Bovine immunoglobulin isotype-specific murine monoclonal antibodies were used in sandwich radioimmunoassays to detect and quantitate bovine IgG1, IgG2, IgM, and IgA in culture fluids. The concentrations of bovine immunoglobulins in unknown samples were extrapolated from standard curves generated with bovine monoclonal immunoglobulins. The lowest detection limits for the bovine immunoglobulin isotypes ranged from 65 to 270 ng/ml.
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Okamoto, Yasuyuki, Noboru Hamada, Toshimichi Fujisawa, Jaeduk Noh, Junichi Yamakawa, Mariko Ohno, Kunihiko Ito e Hirotoshi Morii. "Why no simple relationship between thyroid peroxidase activity-inhibiting immunoglobulins and thyroid function in autoimmune thyroid disease?" Acta Endocrinologica 124, n. 4 (aprile 1991): 442–48. http://dx.doi.org/10.1530/acta.0.1240442.

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Abstract. We have reported that some anti-thyroid peroxidase antibodies inhibit the activity of thyroid peroxidase in vitro. These thyroid peroxidase activity-inhibiting immunoglobulins seem to inhibit thyroid function in some patients, but the relationship between thyroid peroxidase activity-inhibiting immunoglobulins and thyroid function is not simple. We designed this study to explore this lack of a simple relationship. We stained immunoglobulin G deposits by immunofluorescence staining or the peroxidase-antiperoxidase method, and stained endogenous thyroid peroxidase activity by enzyme histochemistry in thyroid sections. When cryostat thyroid sections were incubated with thyroid peroxidase activity-inhibiting immunoglobulins, immunoglobulin G deposits were seen as lines of stain on the apical border and as intracellular staining, and endogenous thyroid peroxidase activity was inhibited. In paraffin-embedded thyroid sections from 5 Hashimoto's patients and 6 Graves' patients, immunoglobulin G deposits were not found on the apical border of the follicular epithelium. In frozen thyroid sections from 22 Graves' patients, no clear deposits of immunoglobulin G on this apical border were seen. In organ-cultured thyroid slices incubated with thyroid peroxidase activity-inhibiting immunoglobulins, endogenous thyroid peroxidase activity was not inhibited. In conclusion, thyroid peroxidase activity-inhibiting immunoglobulins may reach its antigen only with difficulty. This is one of the reasons why no simple relationship is observed between thyroid peroxidase activity-inhibiting immunoglobulins and thyroid function.
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Lock, R. J., e D. J. Unsworth. "Immunoglobulins and immunoglobulin subclasses in the elderly". Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 40, n. 2 (1 marzo 2003): 143–48. http://dx.doi.org/10.1258/000456303763046067.

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Background: Published data imply that adult concentrations are achieved for all Ig isotypes and plateau by 15--18 years of age. Recent data, however, suggest that these results are not applicable in the elderly. There are no equivalent data for IgG subclasses. We present reference range data for an elderly UK patient population, for IgG, IgA, IgM and IgG subclasses. Methods: Serum immunoglobulins were reviewed on samples from 1146 patients > 60 years of age and 925 patients aged 18--60 years. Serum IgG subclasses were reviewed on samples from 498 patients >60 years and 484 patients aged 18--60 years. All Igs and subclasses were measured by nephelometry. Reference ranges were derived by probability plotting. Results: Serum median IgG and IgM concentrations are reduced in the elderly (IgG female P < 0·001, IgG male P < 0·03; IgM female P < 0·001, IgM male P < 0·001). Serum IgA concentrations are maintained. Indeed, men showed a slight increase in serum IgA with age ( P = 0·03). Few differences dependent on gender were seen. Median IgM was lower in men in the younger age groups (18--60 years P < 0·001; 61--70 years P = 0·017). IgG2 is reduced in elderly men ( P = 0·002) and IgG, reduced in elderly women ( P = 0·009). Conclusions: We advocate that centres offering these investigations provide local, method-dependent reference ranges, and suggest an approach as to how this might be achieved.
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Walther, Stefanie, Tamara V. Rusitzka, Ulrike S. Diesterbeck e Claus-Peter Czerny. "Equine immunoglobulins and organization of immunoglobulin genes". Developmental & Comparative Immunology 53, n. 2 (dicembre 2015): 303–19. http://dx.doi.org/10.1016/j.dci.2015.07.017.

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Butler, J. E., e W. R. Brown. "The immunoglobulins and immunoglobulin genes of swine". Veterinary Immunology and Immunopathology 43, n. 1-3 (ottobre 1994): 5–12. http://dx.doi.org/10.1016/0165-2427(94)90114-7.

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Wagner, Bettina. "Immunoglobulins and immunoglobulin genes of the horse". Developmental & Comparative Immunology 30, n. 1-2 (gennaio 2006): 155–64. http://dx.doi.org/10.1016/j.dci.2005.06.008.

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Tesi sul tema "Immunoglobulin A"

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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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Abstract (sommario):
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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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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Hirano, Ayumi. "T dependent B cell help in cattle : immunoregulatory function of interleukin-4 and CD40-CD40L interactions /". free to MU campus, to others for purchase, 1997. http://wwwlib.umi.com/cr/mo/fullcit?p9841150.

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Almroth, Gabriel. "Immunoglobulins, immunoglobulin subclass-distributions and serologic markers in some renal and systemic disorders /". Linköping : Univ, 2000. http://www.bibl.liu.se/liupubl/disp/disp2000/med646s.pdf.

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Rogers, Kenneth Alton. "Immunoglobulins and Immunoglobulin Fc Receptors in Nonhuman Primates Commonly Used in Biomedical Research". Digital Archive @ GSU, 2006. http://digitalarchive.gsu.edu/biology_diss/6.

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Antibodies neutralize and eliminate pathogens, malignancies, and toxins by acting either alone or in association with Fc receptors which, once engaged, activate the elimination mechanisms of phagocytic cells. Based on structural differences, antibodies are divided into functionally distinct classes (IgM, IgD, IgG, IgE and IgA). Structure-function relationships within these classes are not well characterized. In addition, animal models for the assessment of potential therapeutic strategies for the modulation of the interaction between antibodies and Fc receptors are not established. Nonhuman primates are widely used to model human diseases and, represent excellent in vivo systems for this assessment. Therefore, we have studied nonhuman primate IgD as well as IgG and IgA specific Fc receptors in rhesus macaques, cynomolgus macaques, baboons and sooty mangabeys. IgD genes had not been identified in nonhuman primates nor the IgD receptors characterized in any species. We characterized IgD genes of the four monkey species, as well as chimpanzees and dogs. In contrast to other antibody classes, the IgD hinge regions are highly conserved between human and nonhuman primates, thus indicating a role in Fc receptor binding. In humans, Fc receptors CD16a (natural killer cells) and CD16b (neutrophils) bind IgG1 and IgG3, and CD89 (myeloid cells) binds IgA. To assess ligand binding and glycosylation properties of nonhuman primate CD16a, CD16b, and CD89, we sequenced, cloned, and generated recombinant molecules in a mammalian expression system. Our results verify the presence of CD16a, but not CD16b in nonhuman primates. CD16a is expressed on monocytes and a subpopulation of lymphocytes. In sooty mangabeys, CD16 is also expressed on neutrophils. Recombinant sooty mangabey/baboon CD16a binds to human IgG1 and IgG2, but not IgG3 and IgG4. Monkey CD89 has the same peripheral blood leukocyte expression profiles as humans, and binds human and recombinant macaque IgA. Blocking of N-glycans inhibited expression of CD89, but only marginally CD16a expression. Although extensive similarities of antibody/Fc receptor interactions exist between human and nonhuman primates, several differences must be considered when evaluating therapeutic strategies. However, these differences can be exploited to further characterize the structure-function relationships existing within antibody molecules and respective receptors.
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Ding, Cheng. "Siglec-G is a negative regulator of NF-[kappa]B activation and has pivotal roles in B-1 cell development and resistance to sepsis /". Columbus, Ohio : Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1226876722.

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Laurencikiene, Jurga. "Regulation of germline transcription in the immunoglobulin heavy chain locus /". Stockholm, 2004. http://diss.kib.ki.se/2004/91-7349-989-7/.

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Couston, Ruairidh Gair. "Characterising immunoglobulin-polysorbate interactions". Thesis, University of Strathclyde, 2013. http://oleg.lib.strath.ac.uk:80/R/?func=dbin-jump-full&object_id=18963.

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Therapeutic proteins, such as immunoglobulins, are typically formulated with polysorbates as stabilisers. However, the nature of the immunoglobulin-polysorbate interaction, particularly at the solid-liquid interface, is poorly characterised. This thesis presents an investigation of immunoglobulin (mAb-1)-surfactant interaction in bulk solution with particular focus on the interaction at the solid-liquid interface. It was first established using isothermal titration calorimetry that no specific binding interaction between mAb-1 and surfactant in solution takes place. Furthermore, circular dichroism and differential scanning calorimetry showed surfactant inclusion had no effect on mAb-1 native structure or thermal stability. The adsorption/desorption of mAb-1 and the effect of polysorbate was quantified in real-time by total internal reflection fluorescence. MAb-1 desorption was dependent on polysorbate concentration, fatty acid tail group and point of injection relative to mAb-1. MAb-1 adsorption to a hydrophobic surface was significantly less than to a hydrophilic surface. Concomitant conformational changes to mAb-1 were not apparent upon adsorption to a hydrophilic surface but a varying degree of β-sheet loss was observed upon adsorption to hydrophobic surfaces. This was corroborated by neutron reflectivity (NR) data which modelled a bilayer for mAb-1 adsorbed to a hydrophilic surface and a monolayer for mAb-1 adsorbed to a hydrophobic surface. These NR data suggested a range of mAb-1 orientations were adopted. This combination of orthogonal surface analytical techniques can build up a detailed molecular-level image of the adsorbed protein layer enabling rapid characterisation of protein surface adsorption which will improve bioprocess design and formulation.
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Pouria, Shideh. "A study of immunoglobulin A biology in primary and hepatic immunoglobulin A nephropathy". Thesis, King's College London (University of London), 2005. https://kclpure.kcl.ac.uk/portal/en/theses/a-study-of-immunoglobulin-a-biology-in-primary-and-hepatic-immunoglobulin-a-nephropathy(e31804ca-526c-49d0-8767-9110d84f7a4b).html.

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Mason, J. O. "Regulation of immunoglobulin gene expression". Thesis, University of Cambridge, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.384506.

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Libri sul tema "Immunoglobulin A"

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Slayton, Kaetzel Charlotte, a cura di. Mucosal immune defense: Immunoglobulin A. New York: Springer, 2007.

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Slayton, Kaetzel Charlotte, a cura di. Mucosal immune defense: Immunoglobulin A. New York: Springer, 2007.

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1942-, Honjo T., Alt Frederick W e Rabbitts T. H, a cura di. Immunoglobulin genes. London: Academic Press, 1989.

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

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

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Lefranc, Marie-Paule. The immunoglobulin factsbook. San Diego: Academic Press, 2001.

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F, Calabi, e Neuberger, a cura di. Moleculargenetics of immunoglobulin. Amsterdam: Elsevier, 1987.

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Slayton, Kaetzel Charlotte, a cura di. Mucosal immune defense: Immunoglobulin A. New York: Springer, 2007.

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

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F, Calabi, e Neuberger M. S, a cura di. Molecular genetics of immunoglobulin. Amsterdam: Elsevier, 1987.

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Capitoli di libri sul tema "Immunoglobulin A"

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Khelemsky, Yury, Karina Gritsenko e Jason Litt. "Immunoglobulin G". In Pain Medicine, 185–86. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-43133-8_51.

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Pandey, J. P. "Immunoglobulin Genetics". In Immunoglobulins in Health and Disease, 23–29. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4169-4_2.

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Lefranc, Marie-Paule. "Immunoglobulin Synthesis". In Encyclopedia of Systems Biology, 999–1002. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_667.

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Newland, A. C., e P. A. Veys. "Intravenous Immunoglobulin". In Immunotherapy of Disease, 21–42. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-009-1844-3_2.

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Berger, Melvin. "Immunoglobulin products". In Rossi's Principles of Transfusion Medicine, 358–70. Chichester, WestSussex: John Wiley & Sons, Ltd., 2016. http://dx.doi.org/10.1002/9781119013020.ch31.

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Phillips, Derrick. "Intravenous Immunoglobulin". In Handbook of Systemic Drug Treatment in Dermatology, 164–69. 3a ed. London: CRC Press, 2022. http://dx.doi.org/10.1201/9781003016786-24.

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Davis, Elizabeth G. "Immunoglobulin Therapy". In Equine Clinical Immunology, 251–56. Chichester, UK: John Wiley & Sons, Inc., 2015. http://dx.doi.org/10.1002/9781119086512.ch26.

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Gooch, Jan W. "Immunoglobulin (Ig)". In Encyclopedic Dictionary of Polymers, 901. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13997.

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Kipps, Thomas J., Emanuela M. Ghia e Laura Z. Rassenti. "Immunoglobulin Genes". In Manual of Molecular and Clinical Laboratory Immunology, 51–64. Washington, DC, USA: ASM Press, 2016. http://dx.doi.org/10.1128/9781555818722.ch6.

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Banik, Biswajit, e Niraj Arora. "Intravenous Immunoglobulin". In Procedures and Protocols in the Neurocritical Care Unit, 601–16. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-90225-4_28.

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Atti di convegni sul tema "Immunoglobulin A"

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Dichtelmuller, H., e 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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Li, J., e 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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3

Krasnoshtanova, Alla, e 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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4

CAMPANELLA, L., E. MARTINI e M. TOMASSETTI. "COMPARISON BETWEEN TWO DIFFERENT POTENTIOMETRIC METHODS FOR HUMAN ANTI-IMMUNOGLOBULIN G AND HUMAN IMMUNOGLOBULIN G." In Proceedings of the 9th Italian Conference. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812701770_0007.

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Sánchez Montalvo, Alba, Marylene Lecocq, Thomas Plante-Bordeneuve, Caroline Bouzin, Charles Pilette e Valérie Hox. "Polymeric immunoglobulin receptor and immunoglobulin A system in an eosinophilic mouse model of chronic rhinosinusitis". In ERS Lung Science Conference 2022 abstracts. European Respiratory Society, 2022. http://dx.doi.org/10.1183/23120541.lsc-2022.197.

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Decarout, L., M. Hermet e M. Zenut. "DI-025 Intravenous immunoglobulin induced agranulocytosis". In 22nd EAHP Congress 22–24 March 2017 Cannes, France. British Medical Journal Publishing Group, 2017. http://dx.doi.org/10.1136/ejhpharm-2017-000640.272.

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Bezerra, Lia B. M., Letícia K. Dourado, Thiago O. Mencdonça, Telma Antunes e Carmen S. V. Barbas. "Immunoglobulin G Deficiency Associated With Wegener Granulomatosis: Patients Clinical Characteristics And Replacement Therapy With Intravenous Immunoglobulin". In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2990.

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Toti, F., A. Stierlé, M. L. Wiesel, A. Schwartz, J. M. Freyssinet e 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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Chailyan, Anna, Davide Cirillo, Paolo Marcatili e Anna Tramontano. "Structural landscape of immunoglobulin lambda light chains". In the First ACM International Conference. New York, New York, USA: ACM Press, 2010. http://dx.doi.org/10.1145/1854776.1854901.

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Kasavkar, G., e S. Kamath. "AB0399 Rituximab treatment and immunoglobulin levels monitoring". 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.1160.

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Rapporti di organizzazioni sul tema "Immunoglobulin A"

1

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

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2

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

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3

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

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4

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

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5

Block, Timothy M., Songming Chen, Anand S. Mehta e 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, dicembre 2012. http://dx.doi.org/10.21236/ada570851.

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6

Fu, Chengcheng, Xiaohong Wang, Bin Wang, Lingjie Xu e 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, settembre 2021. http://dx.doi.org/10.37766/inplasy2021.9.0086.

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7

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, giugno 2005. http://dx.doi.org/10.21236/ada452454.

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8

Varbanova, Viktoria, Snejina Mihailova, Elissaveta Naumova e 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, luglio 2020. http://dx.doi.org/10.7546/crabs.2020.07.14.

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9

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

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Abstract (sommario):
 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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Chen, Yuhang, Jie Wang, Liqun Wu, Hong Chen e Ziwei Zhang. Efficacy and safety of Chinese herbal medicines in the treatment of allergic rhinitis in children: a systematic review and meta-analysis based on randomized controlled trials. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, aprile 2023. http://dx.doi.org/10.37766/inplasy2023.4.0076.

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Review question / Objective: Population: Children (< 18 years) who were definitively diagnosed with allergic rhinitis were included, without concomitant other diseases. No limitation on location or gender. This study will only consider randomized controlled trials (RCTs) of Chinese herbal medicine for treating patients with allergic rhinitis. Other studies, such as animal studies, reviews, case reports, non-controlled studies, and quasi-RCTs, were not included. Comparison: The control intervention is based on allergic rhinitis treatment guidelines or placebo. Outcome: Primary outcomes: Nasal itching, TNSS, or VAS scores. Secondary outcomes: Effective rates, Serum immunoglobulin E (IgE) level, Serum interleukin (IL - 4, IL - 10, IL - 33) levels, Recurrence rate, and Adverse effects. Study design: This meta-analysis is a secondary study, and the data were extracted from other people's work.
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