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Journal articles on the topic 'Ovalbumin'

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Author: Grafiati

Published: 4 June 2021

Last updated: 1 April 2023

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1

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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2

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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3

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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5

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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11

Lazzarini, Elisa, Andrea Pace, Ilaria Trozzi, Martina Zangheri, Massimo Guardigli, Donato Calabria, and Mara Mirasoli. "An Origami Paper-Based Biosensor for Allergen Detection by Chemiluminescence Immunoassay on Magnetic Microbeads." Biosensors 12, no. 10 (October 4, 2022): 825. http://dx.doi.org/10.3390/bios12100825.

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Food allergies are adverse health effects that arise from specific immune responses, occurring upon exposure to given foods, even if present in traces. Egg allergy is one of the most common food allergies, mainly caused by egg white proteins, with ovalbumin being the most abundant. As allergens can also be present in foodstuff due to unintended contamination, there is a need for analytical tools that are able to rapidly detect allergens in food products at the point-of-use. Herein, we report an origami paper-based device for detecting ovalbumin in food samples, based on a competitive immunoassay with chemiluminescence detection. In this biosensor, magnetic microbeads have been employed for easy and efficient immobilization of ovalbumin on paper. Immobilized ovalbumin competes with the ovalbumin present in the sample for a limited amount of enzyme-labelled anti-ovalbumin antibody. By exploiting the origami approach, a multistep analytical procedure could be performed using reagents preloaded on paper layers, thus providing a ready-to-use immunosensing platform. The assay provided a limit of detection (LOD) of about 1 ng mL−1 for ovalbumin and, when tested on ovalbumin-spiked food matrices (chocolate chip cookies), demonstrated good assay specificity and accuracy, as compared with a commercial immunoassay kit.

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12

Monkos, Karol. "The Glass Transition Temperature and Temperature Dependence of Activation Energy of Viscous Flow of Ovalbumin." Current Topics in Biophysics 39, no. 1 (December 1, 2016): 13–25. http://dx.doi.org/10.1515/ctb-2016-0005.

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Abstract The paper presents the results of viscosity determinations on aqueous solutions of ovalbumin at a wide range of concentrations and at temperatures ranging from 5°C to 55°C. On the basis of these measurements and three models of viscosity for glass-forming liquids: Avramov’s model, free-volume model and power-law model, the activation energy of viscous flow for solutions and ovalbumin molecules, at different temperatures, was calculated. The obtained results show that activation energy monotonically decreases with increasing temperature both for solutions and ovalbumin molecules. The influence of the energy of translational heat motion, protein-protein and protein-solvent interactions, flexibility and hydrodynamic radius of ovalbumin on the rate of decrease in activation energy with temperature has been discussed. One of the parameters in the Avramov’s equation is the glass transition temperature Tg. It turns out that the Tg of ovalbumin solutions increases with increasing concentration. To obtain the glass transition temperature of the dry ovalbumin, a modified Gordon-Taylor equation is used. Thus determined the glass transition temperature for dry ovalbumin is equal to (231.8 ± 6.1) K.

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13

Puspitasari, Wenna, Yuliono NurHasan, and Halida Nelasari. "PENGARUHPEMBERIAN EKSTRAK KUNYIT (CURCUMA LONGA) TERHADAP EKSPRESI SEL GOBLETPADA KONJUNGTIVA TIKUS (RATTUS NOVERGICUS) YANG DIINDUKSI OVALBUMIN." Saintika Medika 12, no. 1 (June 1, 2016): 19. http://dx.doi.org/10.22219/sm.v12i1.5253.

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ABSTRAKKonjungtivitis merupakan sutau peradangan konjungtiva yang ditandai dengan dilatasi pembuluh darah sehingga konjungtiva menjadi hiperemi, edema dan dapat disertai adanya discharge.Curcuminmerupakanbahanaktifdarikunyit yang memilikimanfaatsebagai anti alergi.Penelitian ini bertujuan untuk mengetahuipengaruhpemberianekstrakkunyit (Curcuma longa) terhadapekspresisel goblet padakonjungtivatikus yang diinduksi ovalbumin. PenelitianinimerupakanpenelitianTrue experimentaldenganpost test only group design. Sampeldibagidalamempatkelompokperlakuan yang diberiekstrakkunyitdengandosismasing-masing 35 mg/200grBB, 70 mg/200grBB, 140 mg/200grBB secaraippadaharike 15 dan 18 satu jam sebelumpemberian ovalbumin sertasatukelompokkontrolpositif yang hanyadiberi ovalbumin padaharike 0,7,15 dan 18. Analisis data menggunakanOnewayAnova, bonferonni, kolerasidanregresi.Ekstrakkunyitdapatmenurunkanjumlahsel goblet secarabermakna (ANOVA p=0,000). Terdapathasilujiregresi linier sebesar 70,0%. Dosis minimal yang menunjukkanefeksignifikanadalah 70 mg/kgBB.Ekstrakkunyitberpengaruhterhadappenurunanjumlahsel goblet padakonjungtivatikus (Rattusnorvegicus) yang diinduksi ovalbumin Kata kunci :KonjungtivitisAlergi, Kurkumin, Ovalbumin

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14

Sugimoto, Yasushi, Yoshiki Kamada, Yuhei Tokunaga, Hiroshi Shinohara, Mitsuharu Matsumoto, Takahiro Kusakabe, Takatoshi Ohkuri, and Tadashi Ueda. "Aggregates with lysozyme and ovalbumin show features of amyloid-like fibrils." Biochemistry and Cell Biology 89, no. 6 (December 2011): 533–44. http://dx.doi.org/10.1139/o11-041.

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The interaction of egg-white lysozyme with N-ovalbumin, the native form of egg-white ovalbumin with the denaturation temperature, Tm, of 78 °C, was investigated by the inhibition of lysozyme muramidase activity, differential scanning calorimetry, and circular dichroism assay as indicators. Signals for the interaction were the most prominent when the mixture of lysozyme and N-ovalbumin was co-heated at 72 °C, slightly lower than the Tm of N-ovalbumin. The interaction was also marked when unheated lysozyme was mixed with N-ovalbumin preheated at 72 °C. Moreover, the mixture rapidly formed fibrous precipitates, which were positive for thioflavin T fluorescent emission, a marker for the amyloid fibril formation. Also electron microscopic observation exhibited features of fibrils. The interaction potency of ovalbumin was ascribed to the tryptic fragment ILELPFASGT MSMLVLLPDE VSGLEQLESIINFEK (residues 229–263), derived from the 2B strands 2 and 3 of ovalbumin. From lysozyme, on the other hand, the chymotryptic peptide RNRCKGTDVQAW (residues 112–123), including cluster 6, and the chymotryptic/tryptic peptide GILQINSRW (residues 54–62), including cluster 3, were responsible for the interaction with N-ovalbumin. Interestingly, this nonamer peptide was found to have the ability to self-aggregate. To the authors knowledge, this may be the first report to document the possible involvement of dual proteins in the formation of amyloid-like fibrils.

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15

Fidelio, G. D., B. M. Austen, D. Chapman, and J. A. Lucy. "Interactions of ovalbumin and of its putative signal sequence with phospholipid monolayers. Possible importance of differing lateral stabilities in protein translocation." Biochemical Journal 244, no. 2 (June 1, 1987): 295–301. http://dx.doi.org/10.1042/bj2440295.

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Surface properties of ovalbumin and of its putative signal sequence, and their interactions with phospholipids at an air-water interface, have been studied. The mature protein can form an interfacial film spontaneously from its bulk solution, whereas the signal sequence cannot. Mature ovalbumin also penetrates phospholipid monolayers from the subphase (independently of the type of phospholipid present), whereas its signal sequence does not. The surface stability of a spread film of the signal sequence is, however, higher than that of a film of mature ovalbumin. Above specific threshold concentrations of signal peptide and of mature ovalbumin in mixed films with phospholipids, two separate phases are formed. In such immiscible films, the signal sequence peptide is also able to support a higher lateral surface pressure than mature ovalbumin, at corresponding areas of peptide and mature protein in the mixed monolayers. It is suggested that the differing lateral stabilities of ovalbumin and of its putative signal sequence may be relevant to the translocation of ovalbumin across the membrane of the endoplasmic reticulum, and a scheme for its translocation is proposed that is based on these properties.

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16

Diwan, Deepti, Minaxi Sharma, Meisam Tabatabaei, and Vijai Kumar Gupta. "Ovalbumin production without poultry." Nature Food 2, no. 12 (December 2021): 924–25. http://dx.doi.org/10.1038/s43016-021-00438-y.

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17

Olszowski, S., E. Olszowska, T. Stelmaszyńska, A. Krawczyk, J. Marcinkiewicz, and N. Baczek. "Oxidative modification of ovalbumin." Acta Biochimica Polonica 43, no. 4 (December 31, 1996): 661–72. http://dx.doi.org/10.18388/abp.1996_4462.

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Stimulated neutrophils (PMNL) are a source of the active oxygen species: O2, H2O2 and HOCl/OCl- which in turn can act on proteins yielding a variety of mixed oxidation products. A system is proposed in which a model protein-ovalbumin (OVA) first undergoes chlorination by HOCl/OCl- and next is oxidised by H2O2. The modification of functional groups (-NH2, -SH, -S-S-, > C = O, Tyr and Trp) in OVA was monitored as well as their accessibility to promote aggregation. Chlorination resulted in additional inter- or intra -S-S- bond formation followed by a decrease in the total sulfhydryl group content. Amino groups were oxidised to carbonyl moieties with a concomitant acidic shift of pI. Formation of chlorotyrosine at the chlorination step was confirmed and its further H2O2-mediated transformation to bityrosine was demonstrated. It has also been confirmed that tryptophan, and not tyrosine, is the first target for chlorination. SDS/PAGE and HPLC profiles revealed that HOCl/OCl- chlorination promotes formation of aggregates stabilised by non covalent bonds. In conclusion, we suggest that a dramatic change in the OVA molecule structure begins when the molar excess of HOCl/OCl- is about 2 per one reactive group in OVA.

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18

Onda, Maki, and Masaaki Hirose. "Refolding Mechanism of Ovalbumin." Journal of Biological Chemistry 278, no. 26 (April 23, 2003): 23600–23609. http://dx.doi.org/10.1074/jbc.m300295200.

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19

Orsini, Sibilla, Celia Duce, and Ilaria Bonaduce. "Analytical pyrolysis of ovalbumin." Journal of Analytical and Applied Pyrolysis 130 (March 2018): 62–71. http://dx.doi.org/10.1016/j.jaap.2018.01.026.

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20

Martin, Daniel D., Douglas R. Winters, A. Jeff Mohr, and Bruce G. Harper. "Characterization of Aerosolized Ovalbumin." Aerosol Science and Technology 23, no. 4 (January 1995): 534–40. http://dx.doi.org/10.1080/02786829508965335.

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21

ter Horst, M. G. "The spreading of ovalbumin." Recueil des Travaux Chimiques des Pays-Bas 55, no. 1 (September 3, 2010): 33–42. http://dx.doi.org/10.1002/recl.19360550107.

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22

Gao, Xiao-Pei, Syed R. Akhter, and Israel Rubinstein. "Ovalbumin increases macromolecular efflux from the in situ nasal mucosa of allergic hamsters." Journal of Applied Physiology 84, no. 1 (January 1, 1998): 169–76. http://dx.doi.org/10.1152/jappl.1998.84.1.169.

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Gao, Xiao-Pei, Syed R. Akhter, and Israel Rubinstein.Ovalbumin increases macromolecular efflux from the in situ nasal mucosa of allergic hamsters. J. Appl. Physiol. 84(1): 169–176, 1998.—The purpose of this study was to determine whether bradykinin mediates ovalbumin-induced increase in macromolecular efflux from the nasal mucosa of ovalbumin-sensitized hamsters in vivo and, if so, whether thel-arginine/nitric oxide biosynthetic pathway transduces, in part, this response. We found that suffusion of ovalbumin onto the in situ nasal mucosa of ovalbumin-sensitized hamsters, but not of controls, elicited a significant time- and concentration-dependent increase in clearance of fluorescein isothiocyanate-labeled dextran (mol mass, 70 kDa; P < 0.05). HOE-140, but not des-Arg9,[Leu8]-bradykinin, and N G-l-arginine methyl ester (l-NAME), but not N G-d-arginine methyl ester, significantly attenuated ovalbumin-induced responses.l-Arginine, but notd-arginine, abolished the effects ofl-NAME.l-NAME also significantly attenuated bradykinin-, but not adenosine- induced increase in macromolecular efflux from the in situ nasal mucosa. Overall, these data suggest that ovalbumin increases macromolecular efflux from the in situ nasal mucosa of ovalbumin-sensitized hamsters, in part, by producing bradykinin with subsequent activation of thel-arginine/nitric oxide biosynthetic pathway.

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23

Lee, Bong Ki, Young Gun Yoo, Won Young Lee, Chun Soo Hong, Jae Ku Park, and Jai Youl Ro. "Ovalbumin fused with diphtheria toxin protects mice from ovalbumin induced anaphylactic shock." Yonsei Medical Journal 42, no. 1 (2001): 91. http://dx.doi.org/10.3349/ymj.2001.42.1.91.

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24

Magdassi, S., A. Stawski, and S. Braun. "Grenzflächenspannungserniedrigung durch chemisch modifiziertes Ovalbumin / Interfacial Tension Reduction by Chemically Modified Ovalbumin." Tenside Surfactants Detergents 28, no. 4 (July 1, 1991): 264–66. http://dx.doi.org/10.1515/tsd-1991-280416.

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25

Ben Nasser, Imed, Prosper N. Boyaka, Fatma Fennira Ben Aissa, Moncef Jeddi, and Daniel Tome. "The [173–196] fragment of ovalbumin suppresses ovalbumin-specific rat IgE responses." International Immunopharmacology 3, no. 12 (November 2003): 1569–79. http://dx.doi.org/10.1016/s1567-5769(03)00164-4.

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26

Shi, Xiaolei, Ting Zhang, Xuwen Li, Yu Feng, Xin Tan, and Yongri Jin. "Interaction between tangeretin and ovalbumin to reduce the allergic effects of ovalbumin." Chemical Research in Chinese Universities 32, no. 4 (July 12, 2016): 556–60. http://dx.doi.org/10.1007/s40242-016-6016-7.

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27

Filipovic, Dragana, Marija Radojcic, and Bratoljub Milosavljevic. "Determination of the critical molar mass of ovalbumin oligomers degraded by ultrasound." Journal of the Serbian Chemical Society 65, no. 2 (2000): 123–30. http://dx.doi.org/10.2298/jsc0002123f.

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An experimental method has been developed which enables the determination of the critical molar mass (Mmc) of ovalbumin oligomers degraded by ultrasound of known frequency. To test the validity of the Mmc postulate, a series of ovalbumin oligomers was prepared by the radiolytic cross-linking of 1% solutions of ovalbumin monomer dissolved in 50mMNa/K-phosphate buffer pH 7.0 saturated withN2O. Under these conditions, irradiation with 5 kGy from a 60 Co source, yielded ovalbumin dimers, trimers, tetramers, and higher order oligomers. On the basis of the results obtained with the ovalbumin oligomers, it was concluded that for ultrasound of 23 kHz frequency and 5mm amplitude, the Mmc was 274000 - 14000 g/mol. Our results confirmed that the two postulates in the chemistry of polymer degradation by ultrasound are valid when ovalbumin oligomers are used as substrates, i.e., (1) that the higher the molar mass of the original macromolecule, the faster is its degradation rate, and (2) that a lower molar mass limit (LMmL) exists below which the macromolecules are resistent to further degradation.

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28

Yao, Kunshan, Jun Sun, Jiehong Cheng, Min Xu, Chen Chen, Xin Zhou, and Chunxia Dai. "Development of Simplified Models for Non-Destructive Hyperspectral Imaging Monitoring of S-ovalbumin Content in Eggs during Storage." Foods 11, no. 14 (July 8, 2022): 2024. http://dx.doi.org/10.3390/foods11142024.

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S-ovalbumin content is an indicator of egg freshness and has an important impact on the quality of processed foods. The objective of this study is to develop simplified models for monitoring the S-ovalbumin content of eggs during storage using hyperspectral imaging (HSI) and multivariate analysis. The hyperspectral images of egg samples at different storage periods were collected in the wavelength range of 401–1002 nm, and the reference S-ovalbumin content was determined by spectrophotometry. The standard normal variate (SNV) was employed to preprocess the raw spectral data. To simplify the calibration models, competitive adaptive reweighted sampling (CARS) was applied to select feature wavelengths from the whole spectral range. Based on the full and feature wavelengths, partial least squares regression (PLSR) and least squares support vector machine (LSSVM) models were developed, in which the simplified LSSVM model yielded the best performance with a coefficient of determination for prediction (R2P) of 0.918 and a root mean square error for prediction (RMSEP) of 7.215%. By transferring the quantitative model to the pixels of hyperspectral images, the visualizing distribution maps were generated, providing an intuitive and comprehensive evaluation for the S-ovalbumin content of eggs, which helps to understand the conversion of ovalbumin into S-ovalbumin during storage. The results provided the possibility of implementing a multispectral imaging technique for online monitoring the S-ovalbumin content of eggs.

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29

Dahlman, Anna, Esbjörn Telemo, Staffan Ahlstedt, Lars Å. Hanson, Agnes E. Wold, and Ulf I. Dahlgren. "Immune Response against Ovalbumin in Rats Colonized with an Ovalbumin-Producing Escherichia coli and the Influence of Feeding Ovalbumin." International Archives of Allergy and Immunology 105, no. 4 (1994): 381–85. http://dx.doi.org/10.1159/000236787.

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30

Jayanti, Gatra Ervi, Sri Widyarti, Akhmad Sabarudin, and Sutiman Bambang Sumitro. "EGG WHITE ALBUMIN FORM COMPLEX WITH ASPIRIN AND CAFFEINE AND ITS ROLE AS FREE RADICAL SCAVENGER." Asian Journal of Pharmaceutical and Clinical Research 11, no. 7 (July 7, 2018): 340. http://dx.doi.org/10.22159/ajpcr.2018.v11i7.25440.

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Objective: Egg white protein (ovalbumin) is well known to be freshly consumed in Indonesia as traditional medicine, or it is usually known as “Jamu.” Ovalbumin, as well as egg white albumin, is able to form complex compounds with other substances through the formation of weak chemical and physical bonds. The objective of this study is to understand the behavior of ovalbumin as radical scavenger when it binds to antioxidants such as aspirin and caffeine (as a complex). Methods: In this study, docking sites and ovalbumin as scavenger were studied using computer-modeling software. An ovalbumin was used only for computer modeling, whereas in the wet laboratory, the freeze-drying albumin was used for electron spin resonance (ESR) and Fourier transform-infrared (FTIR) spectroscopy to determine its ability as a scavenger and functional groups, respectively. Albumin solution was applied to measure the viscosity. Results: The variability of tridimensional structures of aspirin was investigated after binding with ovalbumin. However, these structures cannot be seen clearly on caffeine. The root-mean-square deviation analysis showed that aspirin, as well as caffeine, altered the dynamic conformation of ovalbumin. The complex of aspirin-ovalbumin-caffeine which was treated at a temperature of −70°C showed intermolecular force. ESR results showed that the complex compounds could effectively reduce more free radicals when compared to aspirin or caffeine. The existence of aromatic compounds (as confirmed by FTIR) was useful for the scavenger molecules and chemical interaction occurs. The viscosity of the complex was similar with normal gastric mucus, which associated with radical scavenger. Conclusion: The characters of albumin when it binds to aspirin and caffeine indicated that scavenging activity of the complex and the viscosity showed an important result to be physiological scavengers of free radicals.

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Wang, Qian, Min-hsiung Pan, Yi-shiou Chiou, Zhenshun Li, Shudong Wei, Xiaoli Yin, and Baomiao Ding. "Mechanistic understanding of the effects of ovalbumin-nanoliposome interactions on ovalbumin emulsifying properties." LWT 157 (March 2022): 113067. http://dx.doi.org/10.1016/j.lwt.2022.113067.

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Takahashi, Nobuyuki, Eizo Tatsumi, Takuya Orita, and Masaaki Hirose. "Role of the Intrachain Disulfide Bond of Ovalbumin during Conversion into S-Ovalbumin." Bioscience, Biotechnology, and Biochemistry 60, no. 9 (January 1996): 1464–68. http://dx.doi.org/10.1271/bbb.60.1464.

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Abdeladhim, Maha, Ai-Hong Zhang, Laura E. Kropp, Alyssa R. Lindrose, Shivaprasad H. Venkatesha, Edward Mitre, and David W. Scott. "Engineered ovalbumin-expressing regulatory T cells protect against anaphylaxis in ovalbumin-sensitized mice." Clinical Immunology 207 (October 2019): 49–54. http://dx.doi.org/10.1016/j.clim.2019.07.009.

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Huibregtse, Inge L., Veerle Snoeck, An de Creus, Henri Braat, Ester C. de Jong, Sander J. H. van Deventer, and Pieter Rottiers. "Induction of Ovalbumin-Specific Tolerance by Oral Administration of Lactococcus lactis Secreting Ovalbumin." Gastroenterology 133, no. 2 (August 2007): 517–28. http://dx.doi.org/10.1053/j.gastro.2007.04.073.

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Shah, Alok K., Michelle M. Hill, Muhammad J. A. Shiddiky, and Matt Trau. "Electrochemical detection of glycan and protein epitopes of glycoproteins in serum." Analyst 139, no. 22 (2014): 5970–76. http://dx.doi.org/10.1039/c4an00781f.

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Tulyeu, Kumagai, Jimbo, Watanabe, Yokoyama, Cui, Osaka, Mieno, and Yamagata. "Probiotics Prevents Sensitization to Oral Antigen and Subsequent Increases in Intestinal Tight Junction Permeability in Juvenile–Young Adult Rats." Microorganisms 7, no. 10 (October 16, 2019): 463. http://dx.doi.org/10.3390/microorganisms7100463.

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Increased intestinal permeability is thought to underlie the pathogenesis of food allergy. We explore the mechanism responsible for changes in the morphology and function of the intestinal barrier using a rat model of food allergy, focusing on the contribution of intestinal microbiota. Juvenile–young adult rats were sensitized with ovalbumin and treated with antibiotics or probiotics (Clostridium butyricum and Lactobacillus reuteri), respectively. The serum ovalbumin-IgE levels, intestinal permeability, histopathological features, tight junction (TJ)-associated proteins, Th2 cytokines, and gut microbiota in feces were analyzed in each group. Sensitized rats showed an increase in ovalbumin-IgE levels and intestinal permeability with gut mucosal inflammation, whereas rats that received probiotics were only mildly affected. Rats given ovalbumin, but not those given probiotics, showed a reduction in both TJ-related protein expression and localization. Th2 cytokine levels were increased in the sensitized rats, but not in those given probiotics. TJs in rats treated with ovalbumin and antibiotics were disrupted, but those in rats administered probiotics were undamaged. Clostridiaceae were increased in the probiotics groups, especially Alkaliphilus, relative to the ovalbumin-sensitized group. Gut microbiota appears to play a role in regulating epithelial barrier function, and probiotics may help to prevent food sensitization through the up-regulation of TJ proteins.

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Teng, C. S., and C. T. Teng. "Decreased ovalbumin-gene response to oestrogen in the prenatally diethylstilboestrol-exposed chick oviduct." Biochemical Journal 228, no. 3 (June 15, 1985): 689–95. http://dx.doi.org/10.1042/bj2280689.

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Prenatal exposure of the female chick-embryo Müllerian duct to diethylstilboestrol (DES) decreases its future capacity for epithelial tubular-gland-cell differentiation and oviduct ovalbumin-gene expression. Chick Müllerian ducts after prenatal exposure to different concentrations of DES were tested after birth to determine the response of the oviduct toward the oestrogen induction. The quantity of DNA was biochemically determined, the differentiation of tubular-gland cells in the oviduct was studied by light microscopy, and the expression of the ovalbumin gene was detected by hybridization of the total RNA with radioactive ovalbumin cDNA. Comparisons among these three parameters revealed that the expression of the ovalbumin gene was affected most by DES exposure. Exposure to high doses of DES suppressed ovalbumin-gene expression by 75-78%, and inhibited tubular-gland-cell differentiation and thus decreased the DNA content by 29 and 32% respectively. Exposure to low doses of DES caused suppression of ovalbumin-gene expression by 47-53%, but it did not affect the other two parameters. Prenatal DES exposure has strong inhibitory effects on the Müllerian duct at the age (5-8-day-old embryos) when the organ is undifferentiated. Less inhibition is observed when the organ becomes differentiated (15-day-old embryos and older).

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Serre, Karine, Elodie Mohr, Kai-Michael Toellner, Adam F. Cunningham, Samuel Granjeaud, Roger Bird, and Ian C. M. MacLennan. "Molecular differences between the divergent responses of ovalbumin-specific CD4 T cells to alum-precipitated ovalbumin compared to ovalbumin expressed by Salmonella." Molecular Immunology 45, no. 13 (August 2008): 3558–66. http://dx.doi.org/10.1016/j.molimm.2008.05.010.

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39

Kim, Young Kyu, Ju Young Lee, and Han Na Suh. "Cytokine-Induced JAK2-STAT3 Activates Tissue Regeneration under Systemic or Local Inflammation." International Journal of Molecular Sciences 23, no. 4 (February 18, 2022): 2262. http://dx.doi.org/10.3390/ijms23042262.

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We investigated the immune response mechanisms under systemic and local inflammation using mouse models whereby lipopolysaccharide (LPS) was administered intraperitoneally to induce systemic inflammation, and epicutaneous sensitization with ovalbumin was used to induce local inflammation. LPS increased the immune cell infiltration in the cardiac muscle near the aorta, alveoli, hepatic sinusoid, renal interstitium, and the submucosal layer of the duodenum. Similarly, ovalbumin increased the abundance of macrophages in the skin. Both LPS and ovalbumin induced NF-κB p65 and IκBα phosphorylation, as well as the expression of NF-κB target genes (TLR4, IL6, and TNFα). Additionally, both LPS and ovalbumin led to an increase in the absolute IL-1β, IL-6, and TNFα serum levels and cytokine-related janus kinase 2 (JAK2)/signal transducer and activator of transcription 3 (STAT3) phosphorylation. Moreover, the activated JAK2/STAT3 signaling increased the number of Ki67-positive cells (proliferating cells) and development pathway target gene expression (regeneration) in the inflammation models. In conclusion, LPS and ovalbumin increase immune cell infiltration in tissues, NF-κB activation, cytokine levels in serum, cytokine-stimulated JAK2/STAT3 signaling, and tissue regeneration.

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Hirota, Kouichi, Tomomi Kamashima, Seiichi Hashida, and Masayuki Totani. "Immune complex transfer enzyme immunoassay for anti-ovalbumin IgA in serum." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 39, no. 5 (September 1, 2002): 482–86. http://dx.doi.org/10.1258/000456302320314494.

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Background: An immune complex transfer enzyme immunoassay for antiovalbumin immunoglobulin A (IgA) was developed. Methods: Serum-specific antibody was reacted simultaneously with 2,4-dinitrophenyl-bovine serum albumin-ovalbumin conjugate and ovalbumin- β-D-galactosidase conjugate. The complex formed from the three components was trapped onto polystyrene balls coated with anti-2,4-dinitrophenyl group immunoglobulin G, eluted with &epsi; N-2,4-dinitrophenyl-L-lysine and transferred to polystyrene balls coated with anti-human IgA α-chain. Bound β-D-galactosidase activity was determined by fluorometry. Results & Conclusions: The detection limit of this method for the measurement of specific anti-ovalbumin IgA was 9 fmol/tube, which was 20-fold lower than that of the enzyme-linked immunosorbent assay (ELISA). Because serum interference with this method was lower than that with the ELISA, the detection limit of this method was 300-fold lower than that by the ELISA. Anti-ovalbumin IgA was detected in 100% of healthy subjects, which was confirmed by pre-incubation with an excess amount of ovalbumin.

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Chen, Jeng-Chang, Cheng-Chi Chan, Nai-Chun Ting, and Ming-Ling Kuo. "Allergen Exposure in Murine Neonates Promoted the Development of Asthmatic Lungs." Biomedicines 9, no. 6 (June 18, 2021): 688. http://dx.doi.org/10.3390/biomedicines9060688.

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We previously demonstrated that fetal allergen exposure caused T-helper 2 (Th2) cell sensitization. Although neonates are immunologically more mature than fetuses, asthmatic lungs were reportedly mitigated by neonatal allergen administration, mechanically referring to regulatory T-cells and TGF-β signaling but lacking the immunological profiles after neonatal exposure. To reappraise the immunological outcome of neonatal allergen exposure, we injected adjuvant-free ovalbumin intraperitoneally into 2-day-old BALB/c neonates, followed by aerosolized ovalbumin inhalation in adulthood. Mice were examined for the immunological profiles specifically after neonatal exposures, lung function and histology (hematoxylin-eosin or periodic acid Schiff staining), and gene expressions of intrapulmonary cytokines (IL-4, IL-5, IL-13 and IFN-γ) and chemokines (CCL17, CCL22, CCL11 and CCL24). Neonatal ovalbumin exposure triggered Th2-skewed sensitization and ovalbumin-specific IgE production. Subsequent ovalbumin inhalation in adulthood boosted Th2 immunity and caused asthmatic lungs with structural and functional alterations of airways. Gender difference mainly involved airway hyperresponsiveness and resistance with greater female susceptibility to methacholine bronchospastic stimulation. In lungs, heightened chemoattractant gene expressions were only granted to neonatally ovalbumin-sensitized mice with aerosolized ovalbumin stress in adulthood, and paralleled by upregulated Th2 cytokine genes. Thus, aeroallergen stress in atopic individuals might upregulate the expression of intrapulmonary chemoattractants to recruit Th2 cells and eosinophils into the lungs, pathogenically linked to asthma development. Conclusively, murine neonates were sensitive to allergen exposures. Exposure events during neonatal stages were crucial to asthma predisposition in later life. These findings from a murine model point to allergen avoidance in neonatal life, possibly even very early in utero, as the best prospect of primary asthma prevention.

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Hamilton, T. D. C., J. M. Roe, C. M. Hayes, and A. J. F. Webster. "Effect of Ovalbumin Aerosol Exposure on Colonization of the Porcine Upper Airway by Pasteurella multocida and Effect of Colonization on Subsequent Immune Function." Clinical Diagnostic Laboratory Immunology 5, no. 4 (July 1, 1998): 494–98. http://dx.doi.org/10.1128/cdli.5.4.494-498.1998.

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ABSTRACT Seventy-three piglets were weaned at 1 week of age, randomly assigned to 10 groups (A to J), accommodated in stainless steel exposure chambers, and exposed continuously to a controlled environment containing aerosolized ovalbumin. The concentrations of ovalbumin dust were as follows (milligrams per cubic meter): A and F, 16.6; B and G, 8.4; C and H, 4.2; D and I, 2.1; E and J, 0. At weekly intervals, the pigs were bled via venipuncture and anesthetized for nasal lavage and tonsilar biopsies performed for subsequent bacteriologic analysis. At 2 weeks of age, the pigs in groups A to E were challenged with toxigenicPasteurella multocida (108 CFU pig−1), and at 6 weeks of age, the pigs were euthanatized. At postmortem, the extent of turbinate atrophy was assessed on the snout sections by using a morphometric index. Exposure to aerial ovalbumin resulted in a dose-dependent increase in serum antiovalbumin immunoglobulin G (IgG; P < 0.001) and serum antiovalbumin IgA (P < 0.001). Exposure also caused a significant increase in the numbers of P. multocidaorganisms isolated from the upper respiratory tract (P< 0.001) and a corresponding increase in turbinate atrophy, as judged by the morphometric index (P < 0.001). Concurrent challenge with P. multocida and ovalbumin resulted in a significant decrease in both the IgG and IgA responses to ovalbumin (P < 0.001). These results show that ovalbumin exposure increases pig susceptibility to P. multocidacolonization and that toxigenic P. multocida modifies the serum IgG and IgA responses to ovalbumin in the pig. Both of these effects may enhance the virulence of this respiratory pathogen and so influence the pathogenesis of atrophic rhinitis in pigs.

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Hines, K. L., and R. A. Fisher. "Regulation of hepatic glycogenolysis and vasoconstriction during antigen-induced anaphylaxis." American Journal of Physiology-Gastrointestinal and Liver Physiology 262, no. 5 (May 1, 1992): G868—G877. http://dx.doi.org/10.1152/ajpgi.1992.262.5.g868.

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Effects of sensitizing antigen (ovalbumin) on various physiological and hepatic parameters were investigated in sensitized rats and isolated perfused livers derived from sensitized rats. Administration of ovalbumin (500 micrograms) to the portal venous circulation of sensitized but not nonsensitized rats resulted in a rapid and sustained decrease in systemic arterial pressure, characteristic of antigen-induced anaphylaxis, and pronounced increases in hepatic portal pressure and blood glucose concentration. These antigen-mediated alterations were similar to those observed in response to platelet-activating factor (PAF) (0.1 micrograms/kg) administration to rats and were inhibited significantly by specific PAF receptor antagonist WEB 2086 (250 micrograms/kg). Infusion of ovalbumin (3.8 micrograms/ml) into isolated perfused livers derived from sensitized rats resulted in significant increases in hepatic glucose output and portal pressure and decreases in oxygen consumption, as observed in response to PAF (0.28 nM) infusion into perfused livers. These hepatic responses to ovalbumin were antigen specific and were not observed in nonsensitized rat perfused livers. Hemodynamic and glycogenolytic responses to ovalbumin in perfused livers were inhibited significantly but less effectively than similar responses to PAF by infusion of WEB 2086 (500 nM) into livers. Coinfusion of indomethacin (2.8 microM) and nordihydroguariatic acid (1 microM) with WEB 2086 (500 nM) into perfused livers inhibited further hemodynamic but not glycogenolytic responses to ovalbumin. Infusion of nitric oxide (34 microM) into sensitized rat perfused livers prevented the hemodynamic and glycogenolytic responses to both ovalbumin and PAF. These observations provide evidence that hepatic glycogenolysis and vasoconstriction are stimulated during antigen-induced anaphylaxis and suggest that these responses are mediated in part by PAF.

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Schroeder, HE, MRI Khan, WR Knibb, D. Spencer, and TJV Higgins. "Expression of a Chicken Ovalbumin Gene in Three Lucerne Cultivars." Functional Plant Biology 18, no. 5 (1991): 495. http://dx.doi.org/10.1071/pp9910495.

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Routine procedures have been developed for the transformation of lucerne (Medicago sativa cv. Rangelander) with foreign genes using the Agrobacterium tumefaciens binary vector system and for the regeneration of transgenic plants from tissue culture, via somatic embryogenesis. Lucerne transformation was carried out with a gene encoding neomycin phosphotransferase (npt), which conferred resistance to the antibiotic kanamycin, together with a cDNA clone encoding chicken ovalbumin which was modified for expression in plant cells. The ovalbumin cDNA protein coding sequence was combined with the cauliflower mosaic virus 35S promoter and the nopaline synthase 3' flanking sequence to make a chimeric ovalbumin gene. A DNA construct containing both these genes was transferred to lucerne, and ovalbumin was detected in leaves of regenerated plants using protein immunoblots. Pulse-chase labelling experiments and analysis of leaves from the top to bottom of the transformed plants indicated that ovalbumin, once formed, was stable in the leaves of transgenic lucerne. A wide variation in ovalbumin level was frequently observed in plants regenerated from multiple embryos on a single transformed callus. This variation correlated with changes in the restriction enzyme digestion pattern of the ovalbumin DNA from the transgenic plants. These results indicate that each transformed callus may have arisen from more than one transformation event. An alternative interpretation is that the callus may have arisen from a single transformed cell but during cell proliferation the DNA in some cells may have undergone rearrangement prior to embryogenesis. Transformation and regeneration procedures were also developed for two Australian commercial cultivars of lucerne. Although the frequency of recovery of transformed plants was lower than with cv. Rangelander, these protocols open the way for a relatively rapid

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45

Tarayre, J. P., M. Aliaga, M. Barbara, N. Malfetes, and S. Vieu. "Airway Epithelial Cells in Various Models of Bronchial Allergic Inflammation in Guinea Pigs." International Journal of Immunopathology and Pharmacology 5, no. 3 (September 1992): 165–72. http://dx.doi.org/10.1177/039463209200500302.

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The number of airway epithelial cells (AEC) in bronchus lumen after various types of anaphylactic shock of similar intensity was determined in guinea pigs. Aerosol-induced anaphylactic shocks were studied after four types of active sensitization: sensitization by IM injection of 30 mg/kg ovalbumin mixed with Freund's complete adjuvant; sensitization by IM injection of 30 mg/kg ovalbumin; sensitization by IP injection of 1 μg ovalbumin and 50 mg A1 (OH)3 by animal; sensitization by 2 exposures to 1%-ovalbumin aerosol at a 7-day interval. One, 3,6,24 and 48 h after the anaphylactic reaction the number of AEC in bronchoalveolar lavage fluid (BALF) was counted in comparison to guinea pigs sensitized but exposed to 0.9% NaCl aerosol. The number of AEC was significantly increased only 24–48 h after the shock in animals sensitized with ovalbumin in Freund's complete adjuvant. In animals passively sensitized by antiserum obtained with sensitization by ovalbumin in Freund's complete adjuvant and challenged by IV or aerosol administration of antigen, non rise in the number of AEC was obtained 24–48 h after the shock. The higher amount of AEC 24–48 h after the anaphylactic reaction in animals actively sensitized by ovalbumin in Freund's complete adjuvant could be related to the higher increase in the number of neutrophils and of mononuclears obtained in the BALF at these times in comparison to other types of active sensitization. The rise in the number of AEC only after the active reaction seems to show the part played by T-lymphocytes in the induction of this effect. The increase in the number of eosinophils in BALF and the appearance of the hyperreactivity cannot be related to the rise in the AEC in bronchus lumen.

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Magdassi, S., and A. Stawsky. "EMULSIFICATION BY CHEMICALLY MODIFIED OVALBUMIN." Journal of Dispersion Science and Technology 10, no. 3 (January 1989): 213–18. http://dx.doi.org/10.1080/01932698908943171.

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47

Huntington, James A., and Penelope E. Stein. "Structure and properties of ovalbumin." Journal of Chromatography B: Biomedical Sciences and Applications 756, no. 1-2 (May 2001): 189–98. http://dx.doi.org/10.1016/s0378-4347(01)00108-6.

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Durmus, Zehra, Abdulhadi Baykal, Hüseyin Kavas, Mikail Direkçi, and Muhammet S. Toprak. "Ovalbumin mediated synthesis of Mn3O4." Polyhedron 28, no. 11 (July 2009): 2119–22. http://dx.doi.org/10.1016/j.poly.2009.03.026.

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49

Adakudugu, Emmanuel A., David D. Obiri, Elvis O. Ameyaw, Ernest Obese, Robert P. Biney, Douglas B. Aidoo, Isaac T. Henneh, Elizabeth N. Oge, Ama K. Thomford, and Madison Adanusa. "Bergapten modulates ovalbumin-induced asthma." Scientific African 8 (July 2020): e00457. http://dx.doi.org/10.1016/j.sciaf.2020.e00457.

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Konstantinova, Natalie R., and Vladimir I. Lozinsky. "Cryotropic gelation of ovalbumin solutions." Food Hydrocolloids 11, no. 2 (April 1997): 113–23. http://dx.doi.org/10.1016/s0268-005x(97)80019-7.

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