Relevant bibliographies by topics / Ovalbumin

Academic literature on the topic 'Ovalbumin'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 April 2023

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Journal articles on the topic "Ovalbumin"

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Kato, Akio, Atsushi Tanaka, Naotoshi Matsudomi, and Kunihiko Kobayashi. "Deamidation of Ovalbumin durings-Ovalbumin Conversion." Agricultural and Biological Chemistry 50, no. 9 (September 1986): 2375–76. http://dx.doi.org/10.1080/00021369.1986.10867749.

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TAKAHASHI, Nobuyuki, Maki ONDA, Kaori HAYASHI, Masayuki YAMASAKI, Tomoyoshi MITA, and Masaaki HIROSE. "Thermostability of Refolded Ovalbumin andS-Ovalbumin." Bioscience, Biotechnology, and Biochemistry 69, no. 5 (January 2005): 922–31. http://dx.doi.org/10.1271/bbb.69.922.

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KATO, Akio, Atsushi TANAKA, Naotoshi MATSUDOMI, and Kunihiko KOBAYASHI. "Deamidation of ovalbumin during S-ovalbumin conversion." Agricultural and Biological Chemistry 50, no. 9 (1986): 2375–76. http://dx.doi.org/10.1271/bbb1961.50.2375.

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4

Lewis, G. S., S. Wang, and J. B. Taylor. "Responses of pregnant ewes and young lambs to ovalbumin immunization, antiovalbumin antibody transfer to lambs, and temporal changes in antiovalbumin antibody1,2." Translational Animal Science 1, no. 4 (December 1, 2017): 585–91. http://dx.doi.org/10.2527/tas2017.0065.

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Abstract Factors affecting the decay of maternally derived IgG and ability of neonatal lambs to produce protective amounts of their own IgG are not well understood. Thus, we conducted 3 experiments to quantify the 1) response of pregnant ewes to ovalbumin immunization, 2) antiovalbumin antibody (OV-IgG) transfer to lambs, 3) changes over time in OV-IgG in lambs, and 4) response of young lambs to ovalbumin immunization. In Exp. 1, ewes (n = 10/group) either received control (adjuvant + saline) or ovalbumin (ovalbumin + adjuvant + saline) injections at ≈ 42 and 14 d prepartum. Ovalbumin increased (P < 0.001) ewe serum and colostrum OV-IgG. Serum OV-IgG was greater (P < 0.0001) in lambs from ovalbumin-treated than in lambs from control ewes. In Exp. 2, lambs (n = 20/group), which were from ewes that had received ovalbumin prepartum, were given either control or ovalbumin injections on d 1 and 15 of age. From d 1 to 15, maternally derived OV-IgG was less (P < 0.04) in ovalbumin-treated than in control lambs. After d 15, OV-IgG was greater (P < 0.001) in ovalbumin-treated than in control lambs. In Exp. 3, lambs (n = 20/group), which were from ewes naïve to ovalbumin, received 1 of 4 treatments: 1) d-1 + d-15 control injections; 2) d-1 + d-15 ovalbumin; 3) d-28 + d-42 control; and 4) d-28 + d-42 ovalbumin. In d-1 + d-15 ovalbumin lambs, OV-IgG increased (P < 0.001) from d 7 to 21 after treatment and then decreased (P < 0.004) after d 28. In d-28 + d-42 ovalbumin lambs, OV-IgG increased (P < 0.001) steadily until d 21 after treatment and then stabilized after d 21. At ≈ 159 d of age, lambs in each group received injections consistent with their original type. After the d-159 treatment, ovalbumin injection increased (P < 0.0001) OV-IgG, and the injection type × time interaction was significant (P < 0.0001). In d-28 + d-42 ovalbumin lambs, OV-IgG just before the d-159 injections was greater (P < 0.006) than that in the other groups. In this study, late pregnant ewes produced OV-IgG after ovalbumin injections and then transferred OV-IgG to lambs via colostrum. Ovalbumin treatment of young lambs reduced circulating maternally derived OV-IgG, but it also induced an immune response in the lambs. Overall, our results support recommendations to vaccinate ewes against common pathogens during late pregnancy and to ensure that lambs receive adequate colostrum soon after birth.
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Seo, Ji-Hyun, Ju-Woon Lee, Jae-Hun Kim, Eui-Baek Byun, Soo-Young Lee, Il-Jun Kang, and Myung-Woo Byun. "Reduction of allergenicity of irradiated ovalbumin in ovalbumin-allergic mice." Radiation Physics and Chemistry 76, no. 11-12 (November 2007): 1855–57. http://dx.doi.org/10.1016/j.radphyschem.2007.02.094.

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6

Olivier, Celso Eduardo, Daiana Guedes Pinto, Regiane Patussi dos Santos Lima, Mariana Dias da Silva, Raquel Acácia Pereira Gonçalves dos Santos, Ana Paula Monezzi Teixeira, and Patricia Ucelli Simioni. "Assessment of Immunoreactivity against Therapeutic Options Employing the Leukocyte Adherence Inhibition Test as a Tool for Precision Medicine." European Journal of Clinical Medicine 2, no. 3 (June 19, 2021): 40–45. http://dx.doi.org/10.24018/clinicmed.2021.2.3.81.

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Background: The Precision Medicine’s approach employs the endotype concept as a central feature to personalize medical treatment. Individual immunoreactivity, alongside characteristics such as genetics, environment, and diet, is one of the factors that differentiates the therapeutic-driven endotypes. Objective: To evaluate the opportunity of the Leukocyte Adherence Inhibition test to differentiate the immunoreactivity between two similar therapeutic agents employed on Allergen Immunotherapy. Methods: Side by side Leukocyte Adherence Inhibitions tests were performed with ovalbumin and carbamylated ovalbumin on a population of 33 self-reported egg-allergic individuals. Results: The results showed two endotypes inside the immune response of the studied groups: The first endotype was defined by the 16 individuals that presented a significant decrease in ovalbumin’s immunoreactivity after carbamylation (mean of differences = 35%; p = 0.002). The second endotype was defined by 17 individuals that presented a significant increase in ovalbumin’s immunoreactivity after carbamylation (mean of differences = 32%; p = 0.001). Conclusion: The Leukocyte Adherence Inhibition test was able to differentiate two distinct immunoreactivity patterns when comparing two similar therapeutic agents suggesting, as proof of concept, a potential role to be employed as a Precision Medicine tool.
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7

Castellano, Agostina Congiu, Mario Barteri, Antonio Bianconi, and Fabio Bruni. "Conformational Changes Involved in the Switch from Ovalbumin to S-Ovalbumin." Zeitschrift für Naturforschung C 51, no. 5-6 (June 1, 1996): 379–85. http://dx.doi.org/10.1515/znc-1996-5-615.

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Abstract For the first time a comparative study on conformational differences between native oval­ buminand its heat-stable form, called S-ovalbumin. using small angle x-ray scattering, is reported. To detect a different pathway in the folding mechanism of the two proteins, scatter­ing measurements have been performed on ovalbumin and S-ovalbumin denatured with dif­ferent concentrations of guanidine hydrochloride, and by heating the proteins at acid pH. The intensity scattering curves provide evidence that the intermediate states in the unfolding process are globular for both proteins while their compactness changes. The reported experi­mental results suggest that the ovalbumin to S-ovalbumin transformation can be considered a protein-switch triggered by changes in the chemical conditions of the protein environment. Because the conformational changes are likely to be of functional importance, we infer that the occurrence in vivo of S-ovalbumin is thus determined by the transformation of ovalbumin, with a functional role for embryonic development, into a new protein with a dif­ferent function.
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8

Alves, Andrea Catão, Cristiano Machado Gontijo, Mônica Cristina Oliveira, Simone Odília Fernandes Diniz, Flávia Márcia Oliveira, Valbert Nascimento Cardoso, and Gilson Andrade Ramaldes. "Biodistribution of free 99mTc-ovalbumin and 99mTc-ovalbumin encapsulated in liposomes." Brazilian Archives of Biology and Technology 48, spe2 (October 2005): 235–41. http://dx.doi.org/10.1590/s1516-89132005000700035.

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The oral administration of proteic antigens, like ovalbumin, may result in the induction of oral tolerance or immunization. The aim of this work was to label a protein antigen with 99mTechnetium, encapsulate it in liposomes and investigate its absorption and tissue distribution after oral administration in mice. Ovalbumin was labeled with 99mTechnetium and encapsulated in small unilamellar vesicles. 99mTc-OVA encapsulated or not in liposomes was administrated to mice that were sacrificed after different times. The radioactivity was measured in various organs of the animals. Differences concerning the biodistribution of 99mTc-OVA were noticed. The technique may represent alternatives for the induction of immunization or oral tolerance.
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9

Murakami, Kiyofumi. "Kinetics of the Denaturation of Ovalbumin and S-Ovalbumin by Alcohols." Bulletin of the Chemical Society of Japan 61, no. 9 (September 1988): 3043–47. http://dx.doi.org/10.1246/bcsj.61.3043.

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10

Paolinelli, Corrado, Mario Barteri, Federico Boffi, Francesca Forastieri, Maria Cristina Gaudiano, Stefano Della Longa, and Agostina Congiu Castellano. "Structural Differences of Ovalbumin and S-Ovalbumin Revealed by Denaturing Conditions." Zeitschrift für Naturforschung C 52, no. 9-10 (October 1, 1997): 645–53. http://dx.doi.org/10.1515/znc-1997-9-1012.

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We found, by circular dichroism and Raman spectroscopy measurements, that the secondary structure of the native ovalbumin and of its heat-stable form, called S-ovalbumin, is a probe of the structural differences between the two proteins. Small angle X-ray scattering and circular dichroism measurements performed on the two proteins under denaturing conditions, with different concentrations of guanidine hydrochloride, show the changes of the tertiary and secondary structure and a different pathway in the unfolding process. These experimental data confirm that the conversion of native ovalbumin into S-ovalbumin is irreversible and reveal that the response of the two proteins to the same chemical environment is different
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Dissertations / Theses on the topic "Ovalbumin"

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Kremmin, Holger. "Protein-Disassembly im Verlauf der endosomalen Prozessierung." [S.l. : s.n.], 2000. http://ArchiMeD.uni-mainz.de/pub/2001/0006/diss.pdf.

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2

Onda, Maki. "Studies on the Refolding Process of Ovalbumin." Kyoto University, 1999. http://hdl.handle.net/2433/157137.

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本文データは平成22年度国立国会図書館の学位論文(博士)のデジタル化実施により作成された画像ファイルを基にpdf変換したものである
Kyoto University (京都大学)
0048
新制・論文博士
博士(農学)
乙第10251号
論農博第2262号
新制||農||791(附属図書館)
学位論文||H11||N3334(農学部図書室)
UT51-99-T785
(主査)教授 廣瀬 正明, 教授 井上 國世, 教授 北畠 直文
学位規則第4条第2項該当
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3

Shirai, Nobuaki. "Studies on the Folding of Heat-denatured Ovalbumin." Kyoto University, 1997. http://hdl.handle.net/2433/160881.

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本文データは平成22年度国立国会図書館の学位論文(博士)のデジタル化実施により作成された画像ファイルを基にpdf変換したものである
Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第6898号
農博第916号
新制||農||739(附属図書館)
学位論文||H9||N3022(農学部図書室)
UT51-97-H282
京都大学大学院農学研究科食品工学専攻
(主査)教授 安本 教傅, 教授 廣瀬 正明, 教授 佐々木 隆造
学位規則第4条第1項該当
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4

Bezerra, Fernanda Carvalho. "ParticipaÃÃo dos hormÃnios tireoideanos no desenvolvimento de hiperreatividade induzida pelo desafio antigÃnico com ovalbumina em traquÃias isoladas de ratos sensibilizados." Universidade Federal do CearÃ, 2005. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=114.

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Conselho Nacional de Desenvolvimento CientÃfico e TecnolÃgico
Com o objetivo de verificar a influÃncia dos hormÃnios tireoideanos no desenvolvimento de hiperreatividade traqueal, ratos machos (200 - 250 g) eutireÃideos, hipotireÃideos (propiltiouracil [PTU] - v.o. 0,05% p/v, durante 4 semanas) ou hipertireÃideos (L- tiroxina [T4] - 0,5 mg/kg s.c., por 7 ou 9 dias) foram sensibilizados à ovalbumina (OVA) e, 14 dias depois, desafiados atravÃs da inalaÃÃo de OVA (1 mg/ml, seguida de 5 mg/ml, 15 min cada). O sacrifÃcio dos animais para a realizaÃÃo dos experimentos ocorreu 24 h apÃs o desafio antigÃnico por anestesia com hidrato de cloral (400 mg/Kg). A traquÃia isolada foi montada em cubas contendo 10 ml de Krebs-Henseleit modificado (37 oC, 5% de CO2 em O2). Foram obtidas curvas concentraÃÃo-efeito (CCE) para cloreto de potÃssio (KCl), carbacol (CCh) ou serotonina (5-HT). TambÃm foram realizadas CCE ao Ca2+ em preparaÃÃes estimuladas por KCl, CCh ou 5-HT e mantidas em soluÃÃo sem Ca2+. A reapresentaÃÃo do antÃgeno promoveu significativo aumento (p < 0,05, two-way ANOVA) da resposta mÃxima (RM) das CCE ao KCl de 0,96  0,10 gF para 1,53  0,11 gF (n = 7), ao CCh de 1,98  0,06 gF para 2,92  0,07 gF (n = 7) e à 5-HT de 1,64  0,14 gF para 2,41  0,15 (n = 6) nos tecidos obtidos de animais sensibilizados ou desafiados, respectivamente. As traquÃias tambÃm apresentaram aumento (p < 0,05, two-way ANOVA) da RM ao Ca2+ quando estimuladas com KCl de 0,54  0,06 gF para 0,86  0,07 gF (n = 6), com CCh de 1,20  0,14 gF para 1,77  0,14 gF (n = 6) ou com 5-HT de 0,59  0,10 gF para 1,15  0,05 gF (n = 6) nos tecidos obtidos de animais sensibilizados ou desafiados, respectivamente. O hipotireoidismo nÃo alterou significativamente a RM induzida por KCl e CCh, enquanto que aquela induzida pela 5-HT foi reduzida de 1,64  0,14 gF nos animais eutireÃideos para 0,34  0,07 gF nos animais hipotireÃideos (p < 0,001, two-way ANOVA). ApÃs desafio, a 5-HT produziu 0,56  0,11 gF (n = 7) no tecido hipotireÃideo (p < 0,001, two-way ANOVA). O hipotireoidismo aboliu o desenvolvimento de hiperreatividade para KCl e CCh. Ocorreu um aumento na CE50 nas CCE obtidas ao CCh de 0,49 x 10-6M para 4,65 x 10-6M (P < 0,05, two-way ANOVA ). O desafio reduziu a CE50 novamente para 1,53 x 10-6M (n = 6, p<0,05, two-way ANOVA). As traquÃias de animais hipotireÃideos desafiados apresentaram diminuiÃÃo da RM ao Ca2+ quando estimuladas com KCl, CCh e 5-HT. Ocorreu aumento na CE50 nas CCE ao Ca2+ em traquÃias desafiadas e estimuladas com CCh de 5,77 x 10-4 M para 22,50 x 10-4 M (n = 6, p<0,01 two-way ANOVA). O hipertireoidismo promoveu um significativo aumento na RM das CCE apenas ao KCl (0,96  0,10 gF no controle versus 1,58  0,15 no tecido hipertireÃideo). NÃo houve desenvolvimento de hiperreatividade apÃs o desafio antigÃnico (RM = 1,87  0,14 gF). Ocorreu diminuiÃÃo da CE50 ao CCh de 0,67 x 10-4 M no controle para 0,14 x 10-4 M apÃs tratamento com T4. Os resultados mostram que hà envolvimento dos hormÃnios tireoideanos no desenvolvimento de hiperreatividade em traquÃia de rato, induzida apÃs reapresentaÃÃo do antÃgeno a animais previamente sensibilizados.
In other to verify the influence of thyroid hormones on the tracheal hyperreactivity development, euthyroid, hypothyroid (propiltiouracil [PTU] - p.o. 0.05% w/v, 4 weeks) or hyperthyroid (L-tiroxine [T4] â 0.5 mg/kg s.c.,7 or 9 days) male rats (200 - 250 g) were sensitized to ovalbumine (OVA) and, 14 days later, challenged with OVA inhalation, (1 mg/ml, followed by 5 mg/ml, 15 min each). Animals sacrifice was carried out 24 later by means of anaesthesia with chloral hydrate (400 mg/Kg). Isolated trachea was mounted in 10 ml bath chamber filled with modified Krebs-Henseleit (37 oC, 5% de CO2 em O2). Concentration-effect curves (CEC) were carried out for potassium chloride (KCl), carbachol (CCh) or serotonin (5-HT). CEC to Ca2+ added in tissues maintained in Ca2+-free medium stimulated with KCl, CCh or 5-HT also were carried out. Antigenic challenge produced significant increase (p < 0.05, two-way ANOVA) of the maximal response (Emax) of the CCE for KCl from 0.96 Â 0.10 gF to 1.53 Â 0.11 gF (n = 7), for CCh from 1.98 Â 0.06 gF to 2.92 Â 0.07 gF (n = 7) and for 5-HT from 1.64 Â 0.14 gF to 2.41 Â 0.15 (n = 6) in tissues obtained from sensitized or challenged animals, respectively. Tracheae also showed increase on the Emax to Ca2+ (p < 0.05, two-way ANOVA) when stimulated with KCl from 0.54 Â 0.06 gF to 0.86 Â 0.07 gF (n = 6), with CCh from 1.20 Â 0.14 gF to 1.77 Â 0.14 gF (n = 6) or with 5-HT from 0.59 Â 0.10 gF to 1.15 Â 0.05 gF (n = 6) on sensitized or challenged tissues, respectively. The hypothyroidism did not modify significantly the KCl- or CCh-induced Emax, while the 5-HT-induced contractile effect was reduced from 1.64 Â 0.14 gF in euthyroid tissues to 0.34 Â 0.07 gF in hypothyroid tissues (p < 0.001, two-way ANOVA). After challenge, 5-HT produced in hypothyroid tissues a contraction corresponding to 0.56 Â 0.11 gF (n = 7, p < 0.001, two-way ANOVA). Hypothyroidism prevented hyperreactivity development for KCl and CCh. It was observed an increased EC50 value in CCE for CCh from 0.49 x 10-6M to 4.65 x 10-6 M (p < 0,05, two-way ANOVA). After challenge, CE50 value was reduced to 1.53 x 10-6 M (n = 6, p < 0,05, two-way ANOVA). Tracheae from challenged hypothyroid animals showed decreased Emax to Ca2+ when they were stimulated with KCl, CCh and 5-HT. It was observed an increased EC50 value in CCE to Ca2+ in challenged tissues stimulated with CCh from 5.77 x 10-4 M to 22.50 x 10-4 M (n = 6, p < 0.01, two-way ANOVA). Hyperthyroidism significantly increased Emax of the KCl-induced CCE (0.96 Â 0,10 gF in control versus 1.58 Â 0.15 on hyperthyroid tissue). Hyperreactivity was not showed after antigenic challenge (Emax = 1.87 Â 0.14 gF). It was observed a reduction of the EC50 value to CCh from 0.67 x 10-4 M in control to 0.14 x 10-4 M after T4 treatment. Our results show that there is a putative thyroid hormones involvement in hyperreactivity development on rat trachea, after an antigenic challenge.
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Ferreira, Stella da Silva. "Avaliação do potencial erosivo do suco de laranja modificado pela adição de caseína e ovalbumina." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/23/23134/tde-21092011-095114/.

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Nesse estudo in vitro foi avaliado o potencial erosivo do suco de laranja modificado pela adição de caseína, ovalbumina e a combinação entre elas, sobre o esmalte e a dentina humanos. Duas proteínas da dieta, 0.2 g/l de caseína (CAS), 2.0 g/l de ovalbumina (OVA) e a combinação entre elas (CAS + OVA) foram adicionadas a um suco de laranja disponível comercialmente. O suco de laranja sem aditivos foi utilizado como controle negativo (C-) e o suco de laranja com adição de cálcio, também disponível comercialmente, como controle positivo (C+). O potencial erosivo dos sucos experimentais foi primeiramente comparado utilizando o método do pHStat, e em seguida, através de um modelo in vitro de erosão-remineralização. 55 espécimes de esmalte e 55 de dentina radicular (4 x 4 x 2mm) foram obtidos e incluídos em um bloco de resina acrílica. Esses blocos foram então planificados com discos de lixa abrasivos e polidos com disco de feltro e pasta diamantada. As superfícies polidas receberam a aplicação de fitas adesivas, expondo uma janela de 4 x 1mm. Os espécimes foram aleatoriamente distribuídos entre os 5 grupos experimentais (n = 11), e imersos nos respectivos sucos por 5 min, 6x ao dia, durante 5 dias. Entre as imersões e durante o período noturno, os espécimes permaneceram armazenados em saliva artificial. Após a ciclagem, os espécimes de esmalte foram analisados através de perfilometria óptica e microdureza (50 g, 15 s), enquanto que os espécimes de dentina foram analisados apenas por perfilometria óptica. Para o método do pH-Stat foi calculada a média do volume de HCl obtida em triplicata. Para a análise dos dados obtidos através de perfilometria e microdureza, foi utilizado o teste de Análise de Variância, um fator, seguido pelo teste complementar de Tukey, adotando um nível de significância de 5%. As médias do volume de HCl (em ml) obtidas no método do pH-Stat foram: C+ 0,46 (± 0,03); CAS 1,22 (± 0,06); OVA 1,10 (± 0,10); CAS+OVA 1,08 (± 0,01) e C- 1,07 (± 0,02). Na avaliação do esmalte, a perda de estrutura (m) observada foi de: C+ 0,09 (± 0,20); CAS -0,40 (± 0,32); OVA -0,44 (± 0,26); CAS+OVA -0,39 (± 0,25) e C- -1,04 (± 0,36). Quanto a microdureza superficial, os valores de dureza Knoop obtidos foram: C+ 312,68 (± 20,45); CAS 121,99 (± 10,70); OVA 108,87 (± 11,16); CAS+OVA 102,57 (± 11,89) e C- 101,94 (± 8,56). Para a dentina, a perda de estrutura observada foi de: C+ -0,82 (± 0,28); CAS -7,26 (± 0,65); OVA -6,74 (± 1,18); CAS+OVA -7,16 (± 0,75) e C- -7,51 (± 1,26). Conclui-se que para o esmalte, os sucos de laranja modificados pela adição de proteínas apresentaram um potencial erosivo reduzido. A caseína mostrou uma melhor proteção da desmineralização subsuperficial do esmalte; a sua combinação com a ovalbumina não apresentou nenhum benefício adicional. Para a dentina, nenhuma redução no potencial erosivo foi observado para os sucos de laranja modificados pela adição de proteínas.
The erosive potential of a modified orange juice by addition of casein, ovalbumin and its combination, on human enamel and root dentin was evaluated in this in vitro study. Two dietary proteins, 0.2 g/l casein (CAS), 2.0 g/l ovalbumin (OVA) and their combination (CAS + OVA) were added to a commercially available orange juice. The juice with no additives was used as negative control (C-) and a commercially available calcium-modified juice as positive control (C+). The erosive potential of the experimental juices was initially compared by the pH-Stat method, and then, by an in vitro erosion-remineralization cycling model. 55 enamel and 55 root dentin specimens (4 x 4 x 2mm) were obtained and embedded in acrylic resin blocks. These blocks were ground flat with abrasive discs and polished with felt paper and diamond paste. The polished surfaces were covered with an adhesive tape, leaving a central area of 4 x 1mm exposed. The specimens were randomly allocated within the 5 experimental groups (n=11), and immersed in the respective juices for 5 min, 6x/day, for 5 days. Between the immersions and overnight they were stored in artificial saliva. After the cycling, the enamel specimens were analyzed by surface Knoop microhardness (50g, 15s) and optical profilometry, while dentin specimens were analyzed only by profilometry. The mean volume of HCl obtained in triplicate were calculated for the pH-Stat method. The data obtained for profilometry and microhardness were statistically analyzed using ANOVA, one-way, followed by Tukeys test considering a significance level of 5%. The mean volume of HCl (ml) obtained for the pH-stat method were: C+ 0,46 (± 0,03); CAS 1,22 (± 0,06); OVA 1,10 (± 0,10); CAS+OVA 1,08 (± 0,01) e C- 1,07 (± 0,02). For enamel, the surface loss (m) was: C+ 0,09 (± 0,20); CAS -0,40 (± 0,32); OVA -0,44 (± 0,26); CAS+OVA -0,39 (± 0,25) e C- -1,04 (± 0,36). Regarding microhardness, the Knoop hardness values were: C+ 312,68 (± 20,45); CAS 121,99 (± 10,70); OVA 108,87 (± 11,16); CAS+OVA 102,57 (± 11,89) e C- 101,94 (± 8,56). For dentin, the surface loss (m) was: C+ - 0,82 (± 0,28); CAS -7,26 (± 0,65); OVA -6,74 (± 1,18); CAS+OVA -7,16 (± 0,75) and C- -7,51 (± 1,26). It was concluded that protein-modified orange juices presented reduced erosive potential on enamel. Casein showed a better subsurface demineralization protection, and its combination with ovalbumin did not lead to additional benefits. For dentin, any reduction on the erosive potential was observed for protein-modified orange juices.
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6

Farrar, Gabrielle. "Creation of Ovalbumin Based Scaffolds for Bone Tissue Regeneration." Thesis, Virginia Tech, 2009. http://hdl.handle.net/10919/32273.

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Bio-based materials are a viable alternative to synthetic materials for tissue engineering. Although many bio-based materials have been used, Ovalbumin (OA) has not yet been researched to create 3D structures that promote cellular responses. Micro-porous scaffolds are a promising construct for bone tissue regeneration; therefore OA crosslinked with three different concentrations (10%, 15% and 20%) of glutaraldehyde (GA) was used in this research. After fabrication, a porous morphology was observed using SEM. Average pore sizes were found to be comparable to scaffolds previously shown to promote cellular response. A TNBS assay determined percent crosslinking in the scaffolds, however there was no significant difference in percent crosslinking despite differing GA concentrations used. Possible explanations include an excess of GA was used. Using DSC, a glass transition temperature (Tg) was found for control indicating the scaffolds are amorphous. Average dry and wet compressive strengths were also found. As expected, differing GA concentrations had no significant effect on Tg and average compressive strengths due to an excess used. Scaffolds were mechanically tested at 37°C with no significant difference found; therefore these scaffolds can be used in the body. It was shown through cell studies that MC3T3-E1 pre-osteoblast cells significantly increased in number on the 10% and 15% scaffolds, therefore cell proliferation occurred. Because of a positive cellular response, 10% GA scaffolds were used for differentiation studies that showed an increase in osteocalcin at 21 days and alkaline phosphatase levels for scaffolds cultured for 14 days. Overall OA scaffolds have shown to be a promising 3D construct for bone tissue regeneration.
Master of Science
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7

Yamasaki, Masayuki. "Studies on the Conformational Transition of Ovalbumin into Thermostabilized Forms." Kyoto University, 2002. http://hdl.handle.net/2433/149931.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第9645号
農博第1273号
新制||農||847(附属図書館)
学位論文||H14||N3677(農学部図書室)
UT51-2002-G403
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 廣瀬 正明, 教授 池田 篤治, 教授 北畠 直文
学位規則第4条第1項該当
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8

Matoba, Nobuyuki. "Studies on a novel anti-hypertensive peptide derived from ovalbumin." Kyoto University, 2001. http://hdl.handle.net/2433/150784.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第9013号
農博第1195号
新制||農||822(附属図書館)
学位論文||H13||N3532(農学部図書室)
UT51-2001-F343
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 吉川 正明, 教授 佐々木 隆造, 教授 内海 成
学位規則第4条第1項該当
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9

Hannon, Jason Patrick. "Mechanisms of airway hyperreactivity to adenosine induced by allergen challenge in the actively sensitised brown Norway rat." Thesis, Imperial College London, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.312318.

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Castro, Camila Cristina de Lima. "Conjugados de ovalbumina e albumina bovina com desferrioxamina e suas interações com íons metálicos." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/46/46136/tde-21062017-091716/.

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O ferro é essencial para a vida do ser humano, desempenhando um papel fundamental no metabolismo. Contudo, quando não armazenado em compartimentos biológicos adequados, o metal apresenta um potencial tóxico ao organismo, uma vez que contribui para a formação de espécies reativas de oxigênio. A sobrecarga de ferro é uma condição desfavorável para portadores de algumas disfunções genéticas, como a hemocromatose, ou de anemias crônicas que requeiram transfusões de sangue periódicas, como é o caso da talassemia. Os fármacos atuais que controlam a patologia, como a desferrioxamina (DFO), requerem infusão subcutânea lenta, causando desconforto em pacientes e podendo trazer um série de complicações, como insuficiência hepática e renal. A modificação dessas moléculas com biopolímeros é uma proposta para minimizar efeitos colaterais e aumentar a biodisponibilidade do fármaco no organismo. Dentre esses biopolímeros, destacam-se as albuminas proveniente do soro bovino (BSA) e do ovo (OVA), que têm baixa toxicidade, baixo custo e abundância de sítios reativos, que quando modificados, favorecem reação com a desferrioxamina. Como resultado, houve a reação dos biopolímeros com a desferrioxamina, com mudanças em suas estruturas secundárias e possível dimerização, resultando na formação de conjugados possuem afinidade com íon ferro e capacidade antioxidante semelhante ao fármaco original, características que tornam os compostos bons candidatos a uma alternativa à terapia de quelação. Os conjugados BSA-DFO e OVA-DFO podem reagir, além do ferro, com gadolínio, fazendo com o que os complexos tenham uma potencial aplicação como agentes de contraste em ressonância magnética de imagem (MRI). Neste trabalho, vimos que o complexo entre Gd(III) e BSA-DFO apresentou uma relaxatividade de 52,92 s-1 mM-1 para T2 e 45,37 s-1 mM-1 para T1 , um valor bem superior aos fármacos disponíveis no mercado, que apre-sentam relaxatividade entre 4 e 5 s-1 mM-1, o que foi explicado por sua elevada massa molecular, indicando que poderia ter bons efeitos na qualidade de MRI, com menores doses.
Iron is essential for human life, playing a fundamental role in metabolism. However, when not stored in appropriate biological compartments, the metal presents a toxic potential to the body, contributing to the formation of reactive oxygen species (ROS). Iron overload is an unfavorable condition for people with certain genetic disorders, such as hemochromatosis, or chronic anemias that require periodic blood transfusions, as thalassemia. Current drugs that control the pathology, as desferrioxamine, require slow subcutaneous infusion, causing discomfort in patients and may lead to a number of complications, such as hepatic and renal failures. As a result, the biopolymers were reacted with desferrioxamine, with changes in their secondary structures and possible dimerization, resulting in the formation of conjugates with iron ion affinity and antioxidant capacity similar to the original drug, characteristics that make the compounds good candidates for an alternative chelation therapy As a result, the reaction of the biopolymers with desferrioxamine caused a change in the secondary structure, with possible formation of dimers and showing different mobility when exposed to an electric potential difference. Not all polymer chains have reacted with DFO, however BSA-DFO complex has antioxidant capacity similar to the original drug. The BSA-DFO and OVA-DFO conjugates can react, in addition to iron, with gadolinium, making the complexes potential contrast agents for magnetic resonance imaging (MRI). In this work, the complex between Gd(III) and BSA-DFO presented a relaxativity of 52,92 s-1 mM-1 for T2 and 45,37 s-1 mM-1 for T1, values higher than the available drugs in the market (4 - 5 s-1 mM-1) which was explained by the high molecular weight, indicating a good effects on the quality of MRI, with lower doses.
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Books on the topic "Ovalbumin"

1

Carthy, Barry Mc. Ovalbumin, gene Y and serpin inhibitory function. Dublin: University College Dublin, 1998.

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Lutje, Vittoria. Proliferative and antibody responses induced by pokeweed mitogen, sheep erythrocytes and ovalbumin in bovine leukocyte populations, and the cellular interactions involved. Uxbridge: Brunel University, 1989.

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Rozell, Timothy Glenn. Characterization of recombinant ovalbumin-LHRH as a sterilization vaccine. 1993.

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Wang, Zhaohong. Site-directed mutagenesis of chicken ovalbumin upstream promoter transcription factor I (COUP-TFI) in different functional domain. 1997.

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Wang, Zhaohong. Site-directed mutagenesis of chicken ovalbumin upstream promoter transcription factor I (COUP-TFI) in different functional domain. 1997.

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Book chapters on the topic "Ovalbumin"

1

Fujita, Hiroyuki, and Masaaki Yoshikawa. "Vasorelaxing peptide derived from ovalbumin." In Peptide Chemistry 1992, 609–11. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1474-5_175.

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Lechevalier, Valerie, Thomas Croguennec, Françoise Nau, and Catherine Guérin-Dubiard. "Ovalbumin and Gene-Related Proteins." In Bioactive Egg Compounds, 51–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-37885-3_8.

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Morshed, Mahboob, Junko Yamamoto, Shusuke Sano, Ken-Ichi Nishijima, Masamichi Kamihira, and Shinji Iijima. "Biochemical analysis of chicken ovalbumin promoter." In Animal Cell Technology: Basic & Applied Aspects, 301–7. Dordrecht: Springer Netherlands, 2006. http://dx.doi.org/10.1007/1-4020-4457-7_41.

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Daubeuf, F., and Nelly Frossard. "Eosinophils and the Ovalbumin Mouse Model of Asthma." In Methods in Molecular Biology, 283–93. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1016-8_24.

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Du, Liping, Aleš Prokop, and Robert D. Tanner. "Effect of Bubble Size on Foam Fractionation of Ovalbumin." In Biotechnology for Fuels and Chemicals, 1075–91. Totowa, NJ: Humana Press, 2002. http://dx.doi.org/10.1007/978-1-4612-0119-9_87.

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Bowersock, T. L., H. HogenEsch, M. Suckow, John Turek, E. Davis-Snyder, D. Borie, R. Jackson, Haesun Park, and Kinam Park. "Administration of Ovalbumin Encapsulated in Alginate Microspheres to Mice." In ACS Symposium Series, 58–66. Washington, DC: American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0627.ch006.

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Mine, Yoshinori. "Laser-Light-Scattering Properties of Heat-Induced Ovalbumin Gels." In ACS Symposium Series, 104–12. Washington, DC: American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0650.ch008.

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Bianchi, A. T. J., R. J. Zwart, and P. J. van der Heijden. "Induction of a Combined Mucosal and Systemic Anti-Ovalbumin Response." In Advances in Experimental Medicine and Biology, 675–80. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5535-9_101.

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Muramatsu, T., and M. M. Sanders. "Repression of Ovalbumin Gene Expression in the Chicken Oviduct Cell." In Animal Cell Technology: Basic & Applied Aspects, 445–51. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2844-5_61.

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Burapatana, Vorakan, Ernest E. Butler, Gaurav Chauhan, Sean Hartig, Helen Kincaid, Tong Wang, Shayrizal Samsudin, and Robert D. Tanner. "Effect of Lidocaine on Ovalbumin and Egg Albumin Foam Stability." In Biotechnology for Fuels and Chemicals, 905–11. Totowa, NJ: Humana Press, 2003. http://dx.doi.org/10.1007/978-1-4612-0057-4_76.

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Conference papers on the topic "Ovalbumin"

1

Yao, Dong, Bo Xiao, Guiming Zhou, and Biwen Mo. "Icaritin inhibited ovalbumin-induced airway inflammation in murine model." In ERS International Congress 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/13993003.congress-2020.1406.

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Oldenburg, Peter J., Todd A. Wyatt, and Joe H. Sisson. "Alcohol Administration Attenuates Ovalbumin-Induced Airway Hyperresponsiveness In Mice." 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.a4254.

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Wright, David B., Oluwaseun Ojo, Yanira R. Vasquez, Dom Spina, Tak Lee, and Jeremy P. T. Ward. "Heterozygous SERCA2 Knockout Mice In An Ovalbumin Model Of Asthma." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a2236.

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Fu, Lin, Carlos R. Pacheco, Brian Pethica, and R. Prud'Homme. "19F NMR Study of Ovalbumin Diffusion in Guar Filter Cake." In International Symposium on Oilfield Chemistry. Society of Petroleum Engineers, 2007. http://dx.doi.org/10.2118/106461-ms.

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Basu, Sujata, Mark Loewen, Allan B. Becker, and Andrew J. Halayko. "Gender And Age Dependent Airway Responsiveness In Ovalbumin Challenged Mice." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2883.

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Yang, Jun, Jennifer Bratt, Lisa Franzi, Junyan Liu, Guodong Zhang, Hua Dong, Keisha Williams, et al. "Soluble Epoxide Hydrolase Inhibitor Attenuates The Ovalbumin-Induced Murine Asthmatic Symptoms." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1425.

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Tsykhanovska, Irina, Olena Stabnikova, and Sergey Gubsky. "Spectroscopic Studies of Interactions of Iron Oxide Nanoparticles with Ovalbumin Molecules." In IOCN 2022. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/materproc2022009002.

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Song, Renbo, Yujie J. Ding, and Ioulia B. Zotova. "Fingerprinting Ovalbumin - Simulant of Protein Toxins in Extremely-Wide Frequency Range." In Conference on Lasers and Electro-Optics. Washington, D.C.: OSA, 2010. http://dx.doi.org/10.1364/cleo.2010.jwa57.

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Tsurumaki, Hiroaki, Chihiro Mogi, Haruka Saito-Aoki, Koichi Sato, Takashi Nakakura, Masakiyo Yatomi, Yasuhiko Koga, et al. "Absence of proton-sensing TDAG8 protects against ovalbumin-induced allergic airway inflammation." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa2020.

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Baribaud, Frédéric, Huiqing Liu, Patrick Branigan, Daniel Horowitz, Yanqing Chen, Joshua Wertheimer, Joel Tocker, and Matthew Loza. "A murine ovalbumin model exhibits molecular features of steroid insensitive human asthma." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa878.

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Reports on the topic "Ovalbumin"

1

Abeyrathne, Sandun, Hyunyong Lee, and Dong U. Ahn. Sequential Separation of Lysozyme, Ovomucin, Ovotransferrin and Ovalbumin from Egg White. Ames (Iowa): Iowa State University, January 2016. http://dx.doi.org/10.31274/ans_air-180814-234.

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Anderson, Camille O., John M. Prausnitz, and Harvey W. Blanch. Interactions of proteins in aqueous ammonium-sulfate solutions:Mixtures of lysozyme and ovalbumin. Office of Scientific and Technical Information (OSTI), November 2001. http://dx.doi.org/10.2172/861575.

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