Relevant bibliographies by topics / Monoclonial antibodies

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  3. Books
  4. Book chapters
  5. Conference papers
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Academic literature on the topic 'Monoclonial antibodies'

Author: Grafiati
Published: 4 June 2021
Last updated: 19 February 2022

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Journal articles on the topic "Monoclonial antibodies"

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Мерзляк, Е. М., Д. С. Сырко, Е. А. Мусаткина, and М. А. Израельсон. "Использование моноклональных антител для терапии аутоиммунных заболеваний." НАНОМЕДИЦИНА, no. 6 (December 31, 2018): 164–69. http://dx.doi.org/10.24075/vrgmu.2018.094.

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В последнее время в терапии аутоиммунных заболеваний стали применять моноклональные антитела. Мишенью этих антител являются провоспалительные цитокины и собственно Т и В-клетки потенциально участвующие в патогенезе заболевания. В данной статье проведена попытка систематизировать используемые препараты и привести основные механизмы, лежащие в основе такого рода терапии, описаны нежелательные побочные действия. Потенциальными путями и перспективами развития биологиксов в лечении аутоиммунных заболеваний, по нашему мнению, являются моноклональные антитела, которые узнают и элиминируют клоны Т и В-клеток, обусловливающие патогенез аутоиммунного заболевания. Поиск аутореактивных клонов является сложной и актуальной задачей современной биомедицины.
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Choreño-Parra, José Alberto, Martha Carnalla-Cortés, Nayeli Martínez-Zúñiga, and Parménides Guadarrama-Ortíz. "Anticuerpos monoclonales contra el CGRP para el tratamiento de la migraña crónica y episódica." Revista Mexicana de Neurociencia 19, no. 4 (July 1, 2018): 45–61. http://dx.doi.org/10.31190/rmn.2018.19.4.45.61.

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Sela, Michael. "ON THE NOTION OF SYNERGY OF MONOCLONAL ANTIBODIES AS DRUGS." Biotechnologia Acta 6, no. 4 (2013): 16–19. http://dx.doi.org/10.15407/biotech6.04.016.

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Reschova, S., D. Pokorova, Z. Nevorankova, J. Hulova, and T. Vesely. "Detection of spring viraemia of carp virus (SVCV) with monoclonal antibodies." Veterinární Medicína 52, No. 7 (January 7, 2008): 308–16. http://dx.doi.org/10.17221/2043-vetmed.

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Monoclonal antibodies (MAbs) against spring viraemia of carp virus (SVCV), a severe disease in cyprinid fish, were prepared. Nine MAbs were characterised using Western blotting (WB) where all reacted with glycoprotein G, except for MAb 2E1, which showed no reactivity in WB. All nine MAbs showed specificity in an immunoperoxidase test. In ELISA assays, their titres ranged between 1:32 000 and 1:128 000. A panel of SVCV isolates from different European regions were set up and examined by sandwich ELISA assay using the MAbs at a concentration of 15 &mu;g/ml. Only MAb 4C12/3C8 showed low sensitivity in most of the isolates at an absorbance of A<sub>450</sub> the other MAbs, even the lowest absorbance value measured exceeded cut-off for evaluation of the whole reaction. No cross-reaction with the infectious haematopoietic necrosis virus (IHNV), viral haemorrhagic septicaemia virus (VHSV) or infectious pancreatic necrosis virus (IPNV) was demonstrated. 2E1 did not show cross-reactivity with PFRV classified in genogroup III&minus;IV and reacted with a Czech SVCV isolate; its identity was confirmed by means of RT PCR assay. The others MAbs reacted positively with PFRV F4 reference strain, isolated from <i>Esox lucius</i> L. (genogroup III).
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Pekárová-Kyněrová, B., and M. Kutíková. "Preparation and use of monoclonal antibodies to detect Phytophthora nicotianae var. nicotianae." Plant Protection Science 35, No. 2 (January 1, 1999): 41–46. http://dx.doi.org/10.17221/9673-pps.

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A monoclonal antibody (MAb 18) was prepared against purified mycelial proteins from Phytophthora nicotianae var. nicotianae. The specificity of MAb 18 (lgG class) was tested using indirect ELISA (PTA-ELISA).It cross-reacted with Phytophthora cacto­ rum, P. cinrzamomi, P. cryptogea, P. fragariae) but not with other fungi (Fusarium oxysporum, Pythium ultimwn and P. oligan­ drwn) and bacteria (Clavibacter michiganensis subsp. michiganensis) isolated from tomato. Phytophthora nicotianae var. nicotianae was detected in roots and basal stems of artificially infected young tomato plants using indirect ELISA and immunoprinting.
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Reschová, S., D. Pokorová, Z. Nevoránková, and J. Franz. "Monoclonal antibodies to bovine coronavirus and their use in enzymoimmunoanalysis and immunochromatography." Veterinární Medicína 46, No. 5 (January 1, 2001): 125–31. http://dx.doi.org/10.17221/7869-vetmed.

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Two monoclonal antibodies (MAb) to the outer structural protein E2 (spike peplomeric protein) and two MAb to the inner capsid protein N of bovine coronavirus (BCV) were prepared and identified by Western blotting to be used for increasing the specificity and sensitivity of BCV detection. The MAb were checked by the haemagglutination inhibition test and immunoperoxidase tests and no cross reactivity with rotavirus was demonstrated by the immunoperoxidase test and ELISA. A mixture of all the four MAb at predetermined optimum concentrations was first used in sandwich ELISA and then, in combination with an anti‑coronavirus polyclonal antibody, for the development of a simple and rapid immunochromatographic test (ICT). The results of which can be read visually within 10 min. The inclusion of MAb into ELISA and ICT allows the detection of both intact and incomplete BCV virions. ELISA and ICT were used in the examination of a set of 74 faecal samples collected from calves suffering from diarrhoea. ELISA, used as the golden standard verified by electron microscopy, detected BCV in 15 samples (20.3%) and ICT in 16 samples. Three of the ICT‑positive samples were negative by ELISA. On the other hand, two of the 58 ICT‑negative samples were positive by ELISA. Sensitivity and specificity of ICT were 94.9% and 86.7%, respectively
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Израельсон, М. А., А. В. Степанов, Д. Б. Староверов, И. А. Шагина, А. К. Мисорин, А. В. Евстратьева, Е. М. Мерзляк, Е. А. Богданова, О. В. Британова, and С. А. Лукьянов. "Тестирование моноклональных антител к Т-клеточному рецептору, ассоциированному с анкилозирующим спондилитом." ПРОФИЛАКТИЧЕСКАЯ МЕДИЦИНА, no. 5 (December 4, 2018): 83–92. http://dx.doi.org/10.24075/vrgmu.2018.064.

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В последние десятилетия в лечении аутоиммунных заболеваний прослеживается тенденция к замещению симптоматической на молекулярно-таргетную терапию. Предпосылками для этого служат как установленные механизмы развития заболевания, так и прогресс в области биотехнологии. Недавно было показано, что Т-клеточные рецепторы, содержащие вариабельные участки β-цепи TRBV9, ассоциированы со спондилоартропатиями, включая анкилозирующий спондилит. Целью данной работы было получение, определение специфичности и оценка цитотоксичности химерного моноклонального антитела, взаимодействующего с вариабельным участком β-цепи Т-клеточного рецептора, который кодируется генным сегментом TRBV9. С помощью цитометрического анализа, а также массированного секвенирования показано, что химерное антитело обладает высокой специфичностью и цитотоксической активностью. Получение лечебного антитела к потенциально патогенному Т-клону может быть перспективным подходом для терапии аутоиммунных заболеваний в целом и АС в частности.
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Velez, D., J. D. Macmillan, and L. Miller. "Production and use of monoclonal antibodies for identification of Bradyrhizobium japonicum strains." Canadian Journal of Microbiology 34, no. 1 (January 1, 1988): 88–92. http://dx.doi.org/10.1139/m88-018.

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Thirteen murine hybridomas capable of producing monoclonal antibodies to somatic antigens on Bradyrhizobium japonicum were developed and an indirect enzyme-linked immunosorbent assay was used to test reactivity of the antibodies against 20 strains of B. japonicum. Although polyclonal antisera from mice immunized with strains of B. japonicum reacted with bacterial cells of all 20 strains, individual monoclonals were more specific. Some antibodies reacted with as few as 2 and one with as many as 11 strains. On the basis of reactivity with the set of 13 monoclonal antibodies, the 20 strains of B. japonicum could be divided arbitrarily into five groups. Three of five monoclonal antibodies tested reacted with bacteroids taken directly from soybean nodules. One monoclonal bound to cells of five species of Rhizobium, but none of the 13 reacted with gram-negative bacteria representing six other genera. Treatment of cells with reagents and heat indicated the chemical nature of the antigens to five of the monoclonals. Antigen reactive with one antibody was destroyed by periodate oxidation indicating that it was a polysaccharide. Two antigens were probably proteins as they could be digested by trypsin and denatured by heat. Two others were inactivated by all three treatments suggesting they were glycoproteins.
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Vesely, T., S. Reschova, D. Pokorova, J. Hulova, and Z. Nevorankova. "Production of monoclonal antibodies against immunoglobulin heavy chain in common carp (Cyprinus carpio L.)." Veterinární Medicína 51, No. 5 (March 20, 2012): 296–302. http://dx.doi.org/10.17221/5549-vetmed.

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A method for purification of carp serum immunoglobulin (IgM), intended for the production of monoclonal antibodies, was described in the present study. Hybridomas that produce antibodies against IgM heavy chain were selected by ELISA method and Western blotting. Ascitic fluids were prepared and tested by the above mentioned methods, and their typing followed. Monoclonal antibody with the highest titre of antibodies against carp immunoglobulin was selected for conjugation with horseradish peroxidase. Specificity of conjugated monoclonal antibody was tested in a panel of various fish species sera. Cross-reactivity was not detected in rainbow trout (Oncorhynchus mykiss) and eleven other fish species. Besides common carp, positive results were also found in goldfish (Carassius auratus) and bighead carp (Aristichthys nobilis), that are members of Cyprinidae family. Among fish other than Cyprinidae, positive results were also detected in sheatfish (Silurus glanis). The sensitivity in common carp was approximately 10 ng/ml.
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Galkin, O. Yu, O. B. Besarab, Yu V. Gorshunov, and O. M. Ivanova. "New monoclonal antibodies to the Chlamydia trachomatis main outer membrane protein and their immunobiological properties." Ukrainian Biochemical Journal 91, no. 3 (May 15, 2019): 90–98. http://dx.doi.org/10.15407/ubj91.03.090.

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Dissertations / Theses on the topic "Monoclonial antibodies"

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Chen, Desheng, and chen desheng@deakin edu au. "Development of monoclonal antibodies against Vibrio pathogens." Deakin University. Department of Biological Science, 1991. http://tux.lib.deakin.edu.au./adt-VDU/public/adt-VDU20080626.140825.

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Monoclonal antibodies were developed against pathogenic vibrios for use in rapid identification in disease situations of humans, fish and shellfish. Of the 12 fusions performed using V. alginolyticus, V. anguillarum, V. carchariae, V. cholerae, V. damsela, V. furnissii, V. harveyi, V. ordalii, V. parahaemolyticus and V. vulnificus, a total of 102 hybridomas were obtained. Based on cross-reactivity of a wide range of Vibrio strains and other gram-negative bacteria, three broad types of monoclonal antibodies were found. The three categories were: (1) ones that were species-specific or specific to a particular surface antigen, (2) a large number that reacted with several Vibrio species, and (3) three that reacted with most Vibrio strains but no other gram-negative bacteria. Each species-specific monoclonal antibody only recognized its corresponding Vibrio species and was used for identifying unknown species, confirming diagnosis of clinical isolates. In addition, several monoclonal antibodies only cross-reacted with similar Vibrio species, e.g. V. parahaemolyticus and V. alginolyticus which share a common H-antigen. Monoclonal antibodies reacting with several Vibrio species were not of particular use in diagnostic situations. Three monoclonal antibodies of the last group did not react with other genera of the family Vibrionaceae, namely Aeromonas, Photobacterium and Plesiomonas nor a wide range of gram-negative enteric bacteria. These data indicated the existence of an antigenic surface determinant common to Vibrio species. One monoclonal reacted with the heat-stable antigenic determinants on the cell surface as v as lipopolysaccharide extracted from all the vibrios studied, thus making it useful for large- scale screening of acute infections of vibrios. In a blind test, seven Vibrio species, isolated from 6 marine and a freshwater source were identified by two laboratories using phenetic tests. Results of immunotyping using monoclonals, three of seven were diagnosed as the same species, another three were designated as Vibrio species but could not be classified further due to the library not having the corresponding monoclonal, and one was diagnostically questionable. Two further tests were carried out. An unknown Vibrio formalin-fixed isolated from diseased marine animal was identified as V. parahaemolyticus by ELISA and FITC. Clinical human isolates of V. alginolyticus, V. parahaemolyticus and V. vulnificus were confirmed by monoclonals. Australian isolates of V. anguillarum appeared to be mostly of serotype O1. monoclonals raised to V. anguillarum AFHRL 1 reacted with only serotype O1 from Denmark but also most Australian isolates. All vibrios pathogenic to fish and shellfish, i.e. V. anguillarum, V. ordalii, V. alginolyticus, V. carchariae, V. cholerae, V. damsela, V. harveyi, V. parahaemolyticus and V. vulnificus, were used for attachment studies to fish cells using phase contrast and FITC-immunofluorescence microscopy. Of these vibrios, V. anguillarum, V. ordalii and V. perahaemolyticus, were found to adhere to different cells and tissues of rainbow trout while others did not appear to attach. However, attachment was inhibited by monoclonal antibodies specific to only these three vibrios. Lipopolysaccharide is well known as being a contributing factor in pathogenicity of gram-negative bacteria. PAGE electrophoresis of extracted LPS from 9 strains covering 6 Vibrio species showed the presence of a common 15,000 D fragment. This fragment was verified by immunoblotting with a genus-specific monoclonal antibody (i.e. F11P411F) recognizing nearly all vibrios. The common LPS fragment was separated and used to raise polyclonal antisera in mouse which reacted strongly with LPS itself, live as well as sodium azide-killed vibrios, but not with other gram-negative bacteria. This raised the possibility of developing vaccine from Vibrio LPS. Monoclonal antibodies developed in the present study enabled rapid identification of a number of pathogenic Vibrio species. There is still further work to produce monoclonal antibodies against additional vibrios that are probably pathogenic. These included V. fluvialis, V. hollisae, V. metschnikovii, V. minicus, V. salmonella and V. tubiashii. Together the application will be of significance in clinical diagnostic work, in the monitoring of vibriosis in fish farms and in quarantine.
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Austin, Eric B. "Human monoclonal antibodies." Thesis, University of Nottingham, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.276187.

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Plumpton, Christopher. "Monoclonal antibodies against phytochrome." Thesis, University of Cambridge, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.358677.

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Ribeiro, Maricy Alves. ""Contribuição ao imunodiagnóstico da leptospirose humana: ênfase ao uso de anticorpos monoclonais"." Universidade de São Paulo, 2003. http://www.teses.usp.br/teses/disponiveis/9/9136/tde-15032004-161427/.

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A prova sorológica de referência na leptospirose ainda é a soroaglutinação microscópica (SAM). Devido à complexidade desta prova avaliamos alguns testes rápidos para triagem dos anticorpos anti-leptospiras na fase aguda da infecção. Na década de 80, uma hemaglutinação passiva, utilizando frações polissacarídicas de leptospiras, foi considerada apropriada ao diagnóstico precoce, porém esta preparação antigênica incluía muitos “antígenos comuns” reconhecidos por anticorpos de 4% dos indivíduos normais. Um novo ELISA (enzyme-linked immunosorbent assay) utilizando uma suspensão de antígenos imunodominantes, resistentes à proteinase K, foi padronizado e avaliado quanto ao seu valor diagnóstico. Com 89,9% de sensibilidade e 97,4% de especificidade, esta técnica, referida como PK-ELISA, satisfaz os requisitos necessários para as provas de triagem da leptospirose humana. No entanto, em virtude de alguns reagentes usados nesta preparação antigênica serem importados e muito instáveis, foi proposta a introdução de novos métodos empregando-se anticorpos monoclonais. Em um “Acordo de Pesquisa Cooperativa” entre o Instituto Adolfo Lutz e o Laboratório Fleury foram produzidos hibridomas contra leptospiras. Dois deles foram selecionados para dar continuidade ao estudo: um, secretando anticorpos monoclonais (AcM) para um epítopo detectado em 16 de 23 sorovares do gênero Leptospira mais freqüentes em nosso meio (clone A12P4), e outro específico a somente um sorogrupo patogênico, icterohaemorragiae (clone H7P1). O AcM A12P4, uma imunoglobulina G2B (IgG2B), reagiu com epítopo presente nos componentes de pesos moleculares (PM) de 16-18 kDa dos lisados de leptospiras das cepas RGA e M-20, quando separados na eletroforese em gel de poliacrilamida, e com componentes de PM de 75-84kDa dos sorovares copenhageni e canicola. Por sua vez, o AcM H7P1, uma imunoglobulina G, reagiu com um epítopo comum a várias frações de PM acima de 21 kDa da cepa RGA e com componentes de PM de 21-22 kDa e de 75-82 kDa da cepa M-20. Os monoclonais foram empregados em provas imunoenzimáticas para a detecção de anticorpos específicos em amostras séricas pareadas coletadas de 52 pacientes com leptospirose, e do grupo controle que incluiu amostras séricas de 57 pacientes com outras doenças consideradas no diagnóstico diferencial, e de 68 indivíduos normais. Estas provas, no entanto, não foram satisfatórias. Finalmente, um novo ELISA foi desenvolvido no presente estudo que utiliza a suspensão de antígenos “AgMc”, purificados por cromatografia de afinidade utilizando a Sepharose 4B ativada com CNBr acoplada aos anticorpos monoclonais descritos acima. Os resultados obtidos com esta prova foram comparados aos obtidos com outros testes disponíveis em nosso meio, como a SAM e o ELISA clássico (ELISA c). Este novo método, o “ELISA AgMc”, com 80,70 % e 83,33 % de sensibilidade e especifidade, respectivamente, em relação à SAM; valores preditivos positivo e negativo de 69,70% e 90,10% respectivamente e índice de concordância geral de 82,49%, não parece ser um protocolo promissor para o diagnóstico rápido na leptospirose humana. Além disso, tomando-se a SAM como diagnóstico verdadeiro, os resultados obtidos no novo teste, após a conclusão diagnóstica do grupo de pacientes com a leptospirose, mostrou uma discordância significativa. São discutidas as possíveis explicações para os resultados encontrados.
The best serological test for leptospirosis laboratory diagnosis remains the microscopic agglutination test (MAT). Because of the complexity of MAT, we have been developed some rapid screening tests for leptospiral antibodies detection in the acute phase of infection. In the decade of 80, a passive hemagglutination test employing polysaccharide fractions of leptospires was considered appropriate for early diagnosis, but its antigen preparation included “common antigens” recognized by antibodies from 4% of healthy individuals. A new ELISA (enzyme-linked immunosorbent assay) employing proteinase K resistant immunodominant antigens was developed and its potential diagnosis evaluated. This technique, the PK-ELISA, presented 89.9% sensitivity and 97.4% specificity, and satisfied the requeriments needed for serological screening tests of human leptospirosis. However, some of the reagents used in its antigen preparation are imported and very unstable. So, it was proposed, in a “Cooperative Research Accordance” between Instituto Adolfo Lutz and Laboratório Fleury, to try new approaches with monoclonal antibodies. Two hibridomas secreting specific monoclonal antibodies (MAb) were selected: one, against an epitope detected in 16 of 23 members of the genus Leptospira (clone A12P4) and the other, specific to the icterohaemorragiae serogroup (clone H7P1). The MAb A12P4, a G2 (IgG2B) immunoglobulin, reacted with an epitope present in the 16-18 kDa components of icterohaemorragiae serogroup and with the 75-84 kDa components of serovars copenhageni and canicola, after whole-cell lysates of the leptospires were separated by sodium dodecyl sulfate- polyacrylamide gel electrophoresis. The MAb H7P1, which is an IgG, reacted with an epitope common to several fractions of molecular weight above 21 kDa of strain RGA and with the 21-22 kDa and the 75-82 kDa components of strain M-20. Both monoclonal antibodies were employed in enzyme immunoassays for detecting specific antibodies in serum samples serially colleted from 52 patients with leptospirosis, and from the control group, which consisted of sera from 57 patients with other diseases included in the differential diagnosis, and from 68 healthy individuals. These tests, however, were not satisfactory. A new ELISA was developed in the present study employing an antigen suspension “AgMc”, purified by affinity chromatography with CNBr-activated Sepharose 4B coupled to the monoclonal antibodies described above. The results obtained with this test were compared to the MAT and to the classical IgM ELISA (ELISA c). The new method, “AgMc ELISA”, presented serological indices, relatively to reference test MAT, of 80.70 % and 83.33 % of sensitivity and specificity, respectively; positive and negative predictive values of 69.70 % and 90.10 %, respectively, and general agreement index of 82.49 %. So, this test was not considered a promising approach to rapid diagnosis of human leptospirosis. Moreover, the proportion of patients diagnosed as having leptospirosis by the “AgMc ELISA” and the MAT differ significantly. The possible explanations for the results obtained are discussed.
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Qin, Shi-Xin. "Transplantation tolerance with monoclonal antibodies." Thesis, University of Cambridge, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.305697.

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Heron, Andrew David. "The stability of monoclonal antibodies." Thesis, University of Glasgow, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.252169.

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Isaacs, John Dudley. "Improving serotherapy with monoclonal antibodies." Thesis, University of Cambridge, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386115.

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Benjamin, Richard John. "Tolerance induction with monoclonal antibodies." Thesis, University of Cambridge, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.253988.

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Paudel, Subhash. "Shear thinning in monoclonal antibodies." Thesis, Kansas State University, 2016. http://hdl.handle.net/2097/32833.

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Master of Science
Department of Physics
Jeremy D. Schmit
Antibodies are large Y-shaped proteins which are used by immune system to identify and neutralize pathogens. Monoclonal antibody therapy is used to treat different patient conditions. There are problems associated with the manufacturability and deliverability of mAb solutions due to the viscous nature of the protein. The viscosity of antibody solutions increases with the increase in concentration and decreases with applied shear. We want to know why these behaviours are seen and to address this problem we have developed a theory describing the rapid viscosity increase with increasing concentration. We use the polymer theory to explain this behaviour. Here antibodies are treated as polymers. The length of the polymer depend on the aggregation. The reptation time increases approximately as the cubic power of size of aggregate (N³ ). We see the shear thinning behaviour is dependent on the Ab-Ab binding energy and find the relationship between the size of the aggregate and the binding energy. We find aggregate size and morphology using several models for Ab-Ab interaction sites. We use the head to head binding (fAb-fAb binding) model to describe aggregation state in our viscosity theory. The size of the aggregate and hence the reptation time is captured by the binding energy. When the binding energy increases the zero shear viscosity increases and the reptation time decreases. Likewise when the binding energy decreases the zero shear viscosity decreases and the reptation time increases. We have yet to find the correct exponents for the shear thinning behaviour of different mAbs which would be our future work.
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Ueda, Yasuji. "MONOCLONAL ANTIBODIES TO CHICK CRYSTALLINS." 京都大学 (Kyoto University), 1989. http://hdl.handle.net/2433/86412.

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Books on the topic "Monoclonial antibodies"

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Peters, Johann Hinrich, and Horst Baumgarten, eds. Monoclonal Antibodies. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4.

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Ossipow, Vincent, and Nicolas Fischer, eds. Monoclonal Antibodies. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-992-5.

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Albitar, Maher, ed. Monoclonal Antibodies. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-323-3.

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An, Zhiqiang, ed. Therapeutic Monoclonal Antibodies. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2009. http://dx.doi.org/10.1002/9780470485408.

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Steinitz, Michael, ed. Human Monoclonal Antibodies. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8958-4.

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Borrebaeck, Carl A. K., and James W. Larrick, eds. Therapeutic Monoclonal Antibodies. London: Palgrave Macmillan UK, 1990. http://dx.doi.org/10.1007/978-1-349-11894-6.

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Steinitz, Michael, ed. Human Monoclonal Antibodies. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-586-6.

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Sell, Stewart, and Ralph A. Reisfeld, eds. Monoclonal Antibodies in Cancer. Totowa, NJ: Humana Press, 1985. http://dx.doi.org/10.1007/978-1-4612-5176-7.

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Chatenoud, Lucienne. Monoclonal Antibodies in Transplantation. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-662-22195-2.

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Liu, Cheng, and K. John Morrow, eds. Biosimilars of Monoclonal Antibodies. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781118940648.

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Book chapters on the topic "Monoclonial antibodies"

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Peters, J. H., and D. Baron. "Introduction." In Monoclonal Antibodies, 1–17. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_1.

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Peters, J. H., M. Schulze, M. Grol, S. Schiefer, H. Baumgarten, J. Endl, H. Xu, et al. "Demonstration of Monoclonal Antibodies." In Monoclonal Antibodies, 316–461. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_10.

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Baron, D. "Safety Precautions at Work." In Monoclonal Antibodies, 463–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_11.

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Peters, Johann Hinrich, and Horst Baumgarten. "Appendix." In Monoclonal Antibodies, 466–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_12.

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Wiggenhauser, A., J. H. Peters, and H. Baumgarten. "Preconditions for Hybridoma Technology." In Monoclonal Antibodies, 18–38. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_2.

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Baumgarten, H., M. Schulze, J. H. Peters, and T. Hebell. "Immunization." In Monoclonal Antibodies, 39–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_3.

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Wiggenhauser, A., J. H. Peters, H. Baumgarten, and A. Borgya. "Taking Blood and Isolating Cells." In Monoclonal Antibodies, 71–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_4.

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Peters, J. H., E. Debus, H. Baumgarten, R. Würzner, M. Schulze, and Helga Gerlach. "Cell Culture." In Monoclonal Antibodies, 88–136. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_5.

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Baron, D., J. H. Peters, R. K. H. Gieseler, S. Lenzner, H. Baumgarten, R. Würzner, B. Goller, and Th Werfel. "Production of Hybridomas." In Monoclonal Antibodies, 137–222. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_6.

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Baumgarten, H., R. Franze, J. H. Peters, A. Borgya, D. Baron, E. Debus, and M. Kubbies. "Mass Production of Monoclonal Antibodies." In Monoclonal Antibodies, 223–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_7.

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Conference papers on the topic "Monoclonial antibodies"

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Clemetson, K. J., R. Weber, and J. L. McGregor. "TOPOLOGY OF PLATELET GPIb INVESTIGATED BY LOCATION OF MONOCLONAL ANTIBODY EPITOPES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643625.

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A large number of monoclonal antibodies to platelet membrane glycoprotein lb (GPIb) have been described but for most of these the position of the epitope is not known. Since many of these influence platelet function, a better understanding of struc-ture-function relationships requires this knowledge. The position of the epitopes for the monoclonal antibodies API (Dr. T.J. Kunicki), AN51 and SZ-2 (Dr. C-G. Ruan), WM23 (Dr. M.C. Berndt) and PI were determined by analysis of proteolytic cleavage fragments of glycocalicin via affinity chromatography on the monoclonal antibodies coupled to Sepharose, elution with diethyl ami ne solution, separation on SDS-gel electrophoresis and detection by silver-staining. First, intact glycocalicin was examined and was found to bind to all monoclonals with the exception of PI. All monoclonals bound intact GPIb. WM23 bound a 70 kDa glycopeptide from the highly-glycosylated 90 kDa tryptic fragment of glycocalicin. API, AN51 and SZ-2 all bound to 45 kDa and 40 kDa, poorly glycosylated tryptic fragments. The 40 kDa fragment is derived from the 45 kDa fragment and has been shown to be the N-terminal region of GPIb. All these monoclonals have been shown to inhibit von Willebrand factor induced platelet agglutination. Platelets were treated with either elastase or calcium activated protease and monoclonal binding checked by immunofluorescence. The immunofluorescence with API, AN51 and SZ-2 was minimal compared to control platelets whereas that of PI remained as strong as the controls. This indicates that the epitope for PI lies on GPIb in a region other than glycocalicin and its absence from glycocalicin is not simply due to conformational changes in that fragment. Since PI inhibits platelet activation by thrombin and ADP it must act via conformational effects and not by blocking the thrombin receptor which lies on the 45 kDa region of glycocalicin. These results support a more complex role for GPIb in platelet activation.
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Kiefel, V., S. Santoso, and C. Mueller-Eckhardt. "ANALYSIS OF PLATELET REACTIVE ANTIBODIES USING MONOCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643929.

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The characterization of platelet reactive alloantibodies and autoantibodies is mandatory for the diagnosis of posttransfusion purpura, neonatal alloimmune thrombocytopenia, autoimmune thrombocytopenia and for the selection of platelet donors prior to platelet transfusions in immunized polytransfused patients. The platelet immunofluorescence test is suitable for the detection of platelet reactive antibodies. In many cases, however, mixtures containing different platelet reactive antibodies have to be dissected.In order to analyze these sera, we have developed a novel enzyme immunoassay based upon monoclonal antibody specific immobilization of platelet antigens (MAIPA). In brief, platelets are incubated simultaneously with the (human) serum to be investigated and a monoclonal (mouse) antibody directed against an epitope on the same platelet membrane glycoprotein (GP). Platelets are then washed and solubilized in TRIS buffered saline containing NP40. The lysed platelets are then pipetted into the wells of microtiter plates, coated with goat anti mouse IgG where mouse anti GP-complexes are immobilized. Human platelet reactive antibodies on the same GP are detected using enzyme labelled goat anti human IgG, IgM, or IgA, respectively. Using mab Gi5, mab FMC25, mab w6.32 directed against epitopes on the glycoprotein complex IIb/IIIa, glycoprotein Ib and HLA class I molecule, respectively, and a panel of typed platelet donors, even sera containing different platelet reactive antibodies are readily analyzed. Results of experiments with platelet specific alloantibodies (anti P1A1, anti P1A2 and anti Bak(a)), autoantibodies (against the GP Ilb/IIIa complex and GP Ib) and a drug dependent antibody show that this assay allows to discriminate all these different platelet reactive antibodies.
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Hessing, Martin, Joost C. M. Meijers, Jan A. van Mourik, and Bonno N. Bouma. "MONOCLONAL ANTIBODIES TO HUMAN PROTEIN S AND C4b-BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644291.

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Protein S (PS) circulates in plasma both free and in reversible association with the complement component C4b-binding protein (C4bp). Only free PS is functional as a cofactor for activated protein C (APC). Cleavage of PS by thrombin at a site near the r-carboxyglutamic acid domain is associated with a loss of cofactor activity. This may be a control mechanism for the anticoagulant activity of APC. These observations led us to investigate the role of C4bp and thrombin in the regulation of PS. Complex formation between purified PS and C4bp was studied in plasma and in a system with purified components. 125I-labeled PS was first incubated with either C4bp or citrated plasma and then subjected to polyacrylamide gelelectrophoresis in the absence of SDS. The formation of the C4bp-PS complex in plasma and in the purified system was demonstrated by autoradiography. Crossed immuno-electrophoresis using an antiserum against PS was performed in the presence of 8 mM EDTA. Human citrated plasma showed two precipitin peaks. Free PS migrated rapidly in the first dimension, whereas the C4bp-PS complex was just anodal to the application slot. The addition of C4bp to either plasma or purified PS resulted in the disappearance of the free PS peak and an increase of the slower migrating peak. The effect of purified C4bp on the PS-cofactor function of APC was studied in citrated plasma. The prolongation of the APTT induced by the addition of APC could be inhibited by the addition of increasing amounts of C4bp. Monoclonal antibodies to PS and C4bp were prepared and characterized. The monoclonal antibodies to either PS or C4bp did not block the complex formation between and PS, as was demonstrated by dot blotting of C4bp with 125I-PS and agarose gelelectrophoresis followed by Western blotting. Three out of 7 monoclonal antibodies to PS did not detect PS after thrombin cleavage on an immunoblot after non-reduced SDS polyacrylamide gelelectrophoresis. These 3 antibodies gave a significant shortening of the prolonged APTT induced by the addition of APC to normal plasma, indicating that these monoclonals inhibited the cofactor function of PS. The other 4 monoclonals to PS that did detect PS after thrombin cleavage on an immunoblot, gave only a minor inhibition of the PS cofactor function.
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Nomura, S., H. Nagata, N. Sone, K. Oda, T. Kokawa, and K. Yasunaga. "ANALYSIS OF PLATELET ANTIGENS FOR ANTI-PLATELET ANTIBODIES IN ITP USING FLOW CYTOMETRY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644582.

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Idiopathic thrombocytopenic purpura (ITP) is a syndrome caused by circulating antibodies reactive with the platelet membrane. The antigenic specificity of these antibodies is unknown. We have characterized new monoclonal antibodies that react with a determinant specific to GP Ib and GP Ib- Ia complex, and used flow cytometry to investigate platelets in ITP for antigenic determinants to which autoantibodies are directed. Forty cases of ITP were analyzed in detail by the platelet suspension immunofluorescence test(PSIFT) of von dem Borne et al. The monoclonal antibodies used were 5 against GP Ib-Ia complex (NNKY1-32, NNKY2-5, NNKY2-6, NNKY2-11, NNKY2-18) and 2 against GP lb (NNKY5-4, NNKY5-5). The reactivity of monoclonal antibodies was inhibited by the presence of autoantibody on platelets in some ITP patients. Differences in inhibition were found not only between monoclonal antibodies but also between cases.These results suggest that some ITP patients have circulating antibodies to GP Ib or GP II b - Ia, and that heterogeneous antibodies are present on platelets. Moreover, the presence of these autoantibodies may aggravate or initiate a bleeding tendency.
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Yang, Wu, Li-ming Wang, Zhao Wei, and Yuan Junlin. "Preliminary Production of Anti- Glufosinate Monoclonal Antibodies." In 2007 1st International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2007. http://dx.doi.org/10.1109/icbbe.2007.18.

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Metzelaar, M. J., H. K. Nieuwenhuis, and J. J. Sixma. "DETECTION OF ACTIVATED PLATELETS WITH MONOCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643829.

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Blood tests reflecting in-vivo activation of platelets are potentially useful in evaluating patients with thrombotic diseases. Recently monoclonal antibodies have been described that react preferentially with activated platelets. We prepared an IgG2b antibody, designated RUU-AP 2.28, that reacted with a 53.000 MW protein that is located in a special subclass of platelet granules in unstimulated platelets and that is exposed on the surface of activated platelets. Increased numbers of platelets that expressed the 2.28 antigen on their surface were observed in patients undergoing cardiopulmonary bypass and in patients with acute deep venous thrombosis. The percentage of RUU-AP 2.28 positive platelets in the circulation was 3,9 ± 2.7 (SD)% in the controls, (n = 20), 24.6 ± 13.5% in patients after cardiopulmonary surgery (n = 10) and 8.5% in patients with acute deep venous thrombosis (n = 2).In order to detect also earlier stages of platelet activation, such as secretion-independent phenomena, we produced new monoclonal antibodies by fusing spleen cells from Balb/c mice, immunized with thrombin stimulated, paraformaldehyde fixed platelets, with Ag 8653 myeloma cells. As a screening assay we used an ELISA with freshly fixed platelets or fixed thrombin-activated platelets. We detected six monoclonal antibodies (RUU-AP 1-6) specific for thrombin-activated platelets. The results of the ELISA were confirmed by flow cytofluorometry.None of the antibodies inhibited platelet aggregation induced by ADP, collagen or ristocetin. Ascites of IgGl antibody RUU-AP 3 reacted with normal thrombin-activated platelets but did not react with thrombin-activated platelets from a patient with Glanzmann’s disease. In addition antibody RUU-AP 3 reacted with normal platelets stimulated with 1 pM of ADP. These data suggest that antibody RUU-AP 3 detects a secretion-independent conformational change in the platelet membrane glycoprotein IIb-IIIa complex.
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Young, Colin R., Alice Lee, and Larry H. Stanker. "Detection of Campylobacter species using monoclonal antibodies." In Photonics East (ISAM, VVDC, IEMB), edited by Yud-Ren Chen. SPIE, 1999. http://dx.doi.org/10.1117/12.335779.

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Brown, Michael C., Ross Chambers, Dale V. Onisk, Tony R. Joaquim, Lewis J. Stafford, Klaus Lindpaintner, Daniel Keter, and James W. Stave. "Abstract 4325: Monoclonal antibodies to transmembrane proteins." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4325.

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Ray, Jason C., Penelope Allen, Ann Bacsi, Julian Bosco, Luke Chen, Michael Eller, Lyndell Lim, et al. "076 Inflammatory complications of CGRP monoclonal antibodies." In ANZAN Annual Scientific Meeting 2021 Abstracts. BMJ Publishing Group Ltd, 2021. http://dx.doi.org/10.1136/bmjno-2021-anzan.76.

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Berkner, J. A., G. Mitra, and J. W. Bloom. "MONOCLONAL ANTIBODY BINDING TO FACTOR VIII:C." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644063.

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The interactions of monoclonal antibodies with highly purified Factor VIII:c have been studied utilizing the ELISA technique. ELISA plates were coated with Factor VIII:c, protein A purified monoclonal IgG was then added and bound antibody detected with peroxidase labeled antimouse IgG. A Scatchard-Sips plot approach to data analysis was used to calculate binding constants. The binding constants for four antibodies designated BD10, AD7, C7F7 and 39MH8 were as follows: BD10, KO = 7.1 x 108 M-1, n = 1.1 (moles antibody/moles ligand); AD7, KO = 3.1 x 108 M-1, n = 2.7; C7F7, KO = 3.6 x 1011M-1, n = 0.03; 39MH8, K = 6.0 x 1011 M-1, n = 0.03. The binding constants for C7F7 to the purified carboxy-terminal (residues 1649-2332) 80 kD functional region of the Factor VIII:c molecule were also determined: KO = 1.0 x 1011 M-1, n = 0.55. On the basis of these results the following conclusions can be drawn: 1) the antibodies can be divided into two groups: high affinity (suitable for use in immunopurification), C7F7 and 39MH8; low affinity: BD10 and AD7; 2) the antibodies in the low affinity group have valance values two orders of magnitude higher than the high affinity antibodies, C7F7 and 39MH8. The difference might be explained by the high affinity antibody epitopes on the immobilized Factor VIII:c being less exposed to the solution; 3) C7F7 binding to the 80 kD polypeptide, compared to the whole Factor VIII:c molecule, gave virtually identical Kc values, but dramatically different valance values. This suggests that the C7F7 epitope is more accessible on the 80 kD polypeptide.
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Reports on the topic "Monoclonial antibodies"

1

Snyder, Christopher M., and Lawrence J. Wysocki. Dissecting Immunogenicity of Monoclonal Antibodies. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada407659.

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Snyder, Christopher M., and Lawrence J. Wysocki. Dissecting Immunogenicity of Monoclonal Antibodies. Fort Belvoir, VA: Defense Technical Information Center, June 2003. http://dx.doi.org/10.21236/ada417364.

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Jaszczak, R. J. SPECT assay of radiolabeled monoclonal antibodies. Office of Scientific and Technical Information (OSTI), February 1992. http://dx.doi.org/10.2172/7197646.

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Jaszczak, R. J. SPECT assay of radiolabeled monoclonal antibodies. Office of Scientific and Technical Information (OSTI), February 1992. http://dx.doi.org/10.2172/7288347.

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Chia, John K. Polymyxin B(PMB)-Specific Monoclonal Antibodies. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada231817.

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Ivy, John M. Production of Anti-Ferret IgA Antibodies; and production of monoclonal antibodies. Fort Belvoir, VA: Defense Technical Information Center, April 1994. http://dx.doi.org/10.21236/ada279534.

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Sato, J. D. Receptor Monoclonal Antibodies that Inhibit Tumor Angiogenesis. Fort Belvoir, VA: Defense Technical Information Center, August 2001. http://dx.doi.org/10.21236/ada398146.

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Sato, J. D. Receptor Monoclonal Antibodies that Inhibit Tumor Angiogenesis. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada383129.

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Glassy, Mark C. Neutralizing Monoclonal Antibodies against Biological Toxins. Phase 1. Fort Belvoir, VA: Defense Technical Information Center, August 1993. http://dx.doi.org/10.21236/adb176298.

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Jaszczak, Ronald, J. Final Progress Report: SPECT Assay of Radiolabeled Monoclonal Antibodies. Office of Scientific and Technical Information (OSTI), September 2004. http://dx.doi.org/10.2172/886018.

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