Studies on Ovalbumin. IV. Trypsin Digsestion and the Cystine Peptides of Ovalbumin and S-Ovalbumin [PDF]
Australian Journal of Biological Sciences, 1968 Conditions for obtaining comparable tryptic digests of denatured, alkylated ovalbumin and S-ovalbumin have been studied. The tryptic peptides soluble at pH 4 -5 were fractionated by gel filtration in 1 % formic acid. The cystine-peptide fraction was resolved into two cystine peptides by chromatography on DEAESephadex, and by amino acid analyses these ...
MB Smith, Joan F Back
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Studies on Ovalbumin. III. Denaturation of Ovalbumin and S-Ovalbumin [PDF]
Australian Journal of Biological Sciences, 1968 Ovalbumin and S-ovalbwnin have been compared by measuring their viscosity and optical rotatory dispersion in aqueous formamide solutions at pH 7 and in urea solutions at pH 3 5; also by measuring the optical rotatory dispersion of heated solutions at different salt concentrations, and by a study of ultraviolet differlilnce spectra in alkylamine ...
Joan F Back, MB Smith
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Liberation of Carboxyl Groups on Conversion of Ovalbumin tos-Ovalbumin [PDF]
Agricultural and Biological Chemistry, 1981 Titration curves of ovalbumin and s-ovalbumin were compared in studies of changes in properties of ovalbumin on conversion to s-ovalbumin. Although there are 49 carboxyl groups in ovalbumin, two were not titrated in 0.25 M KCl but on conversion to s-ovalbumin.
Shinji Shitamori +2 more
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Studies on Ovalbumin II. The Formation and Properties of S-Ovalbumin, a More Stable Form of Ovalbumin [PDF]
Australian Journal of Biological Sciences, 1965 Ovalbumin is changed to a more stable form (S-ovalbumin) during the storage of shell eggs. Conversion also occurs in an isolated ovalbumin solution, the rate increasing with pH and temperature. First order rate constants for the reaction have been measured at pH 9-10 and at temperatures between 20 and 50 C.
MB Smith, Joan F Back
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Self-assembling nanoparticles containing dexamethasone as a novel therapy in allergic airways inflammation. [PDF]
, 2013 Nanocarriers can deliver a wide variety of drugs, target them to sites of interest, and protect them from degradation and inactivation by the body. They have the capacity to improve drug action and decrease undesirable systemic effects.
Bratt, Jennifer M +6 more
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Immunogenicity of targeted lentivectors [PDF]
, 2014 To increase the safety and possibly efficacy of HIV-1 derived lentivectors (LVs) as an anti-cancer vaccine, we recently developed the Nanobody (Nb) display technology to target LVs to antigen presenting cells (APCs).
Adotévi +67 more
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The role of the tachykinin NK1 receptor in airway changes in a mouse model of allergic asthma [PDF]
, 2004 A
De Swert, Katelijne +3 more
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Protein droplet actuation on superhydrophobic surfaces: A new approach toward anti-biofouling electrowetting systems [PDF]
, 2017 © 2017 The Royal Society of Chemistry. This is an Open Access article, distributed under the terms of the Creative Commons Attribution 3.0 Unported (CC BY 3.0) licence https://creativecommons.org/licenses/by/3.0/.Among Lab-on-a-chip techniques, Digital ...
Abdul Latip, Eli Nadia +6 more
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Some Differences Noted between the Properties of Ovalbumin and s-Ovalbumin in Native State [PDF]
Agricultural and Biological Chemistry, 1980 To study the mechanism of the formation of the heat-stable form of ovalbumin (s-ovalbumin), comparisons were made about the properties of ovalbumin and s-ovalbumin in native state. Although gross structural difference could not be found, some minor differences were clearly noted in some cases such as the DEAE-cellulose chromatographic elution pattern ...
Ryo Nakamura +2 more
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Kinetics of the Denaturation of Ovalbumin and S-Ovalbumin by Alcohols [PDF]
Bulletin of the Chemical Society of Japan, 1988 Abstract The kinetics of denaturation of ovalbumin and S-ovalbumin by butyl alcohol isomers (butyl alcohol, isobutyl alcohol, s-butyl alcohol, and t-butyl alcohol) have been studied. The reactions were characterized as first order with respect to the protein and 11th order for the alcohols, irrespective of the kind of protein or alcohol.
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