Results 261 to 270 of about 74,013 (291)
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Thermostability of Refolded Ovalbumin andS-Ovalbumin
Bioscience, Biotechnology, and Biochemistry, 2005Ovalbumin, a member of the serpin superfamily, is transformed into a thermostabilized form, S-ovalbumin, during storage of shell eggs or by an alkaline treatment of the isolated protein (DeltaT(m)=8 degrees C). As structural characteristics of S-ovalbumin, three serine residues (Ser164, Ser236 and Ser320) take the D-amino acid residue configuration ...
Nobuyuki, Takahashi +5 more
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Monoclonal antibodies against ovalbumin
Biochemical and Biophysical Research Communications, 1981Abstract Fusion of cells of the NS-1 mouse myeloma line with spleen cells from BALB c mice immunized against ovalbumin produced hybrid cells which continuously secrete antibodies specific for ovalbumin. One of these cells was used to establish a cloned line.
Bjercke, R J +3 more
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Archives of Biochemistry and Biophysics, 1961
Abstract A study of the carbohydrate component of ovalbumin points to the presence of three moles of d -glucosamine and six moles of d -mannose per 45,000 g. of the protein. Ovalbumin is extensively oxidized by sodium periodate, the primary reaction with the carbohydrate moiety cleaving three residues of d -mannose and one residue of d ...
Y C, LEE, R, MONTGOMERY
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Abstract A study of the carbohydrate component of ovalbumin points to the presence of three moles of d -glucosamine and six moles of d -mannose per 45,000 g. of the protein. Ovalbumin is extensively oxidized by sodium periodate, the primary reaction with the carbohydrate moiety cleaving three residues of d -mannose and one residue of d ...
Y C, LEE, R, MONTGOMERY
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Nature, 1947
A FEW months ago when working up slops of salt-free iso-electric ovalbumin solutions from half a year of experiments, we made the surprising observation that the protein, when crystallized with ammonium sulphate, appeared as beautiful rectangular plates instead of the usual flat cigar-shaped needles. We did not at that time observe any infection of the
K, LINDERSTROM-LAND, M, OTTESEN
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A FEW months ago when working up slops of salt-free iso-electric ovalbumin solutions from half a year of experiments, we made the surprising observation that the protein, when crystallized with ammonium sulphate, appeared as beautiful rectangular plates instead of the usual flat cigar-shaped needles. We did not at that time observe any infection of the
K, LINDERSTROM-LAND, M, OTTESEN
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Structure and properties of ovalbumin
Journal of Chromatography B: Biomedical Sciences and Applications, 2001Ovalbumin is a protein of unknown function found in large quantities in avian egg-white. Surprisingly, ovalbumin belongs to the serpin family although it lacks any protease inhibitory activity. We review here what is known about the amino acid sequence, post-translational modifications and tertiary structure of ovalbumin.
J A, Huntington, P E, Stein
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A Raman difference spectroscopic investigation of ovalbumin and S‐ovalbumin
Biopolymers, 1979AbstractRaman spectra from 800 to 1850 cm−1 of aqueous solutions of ovalbumin and its more heat‐stable form, S‐ovalbumin, are presented. A Raman difference spectrum (ovalbumin minus S‐ovalbumin) shows differences in intensity in the amide I and III regions. These intensity differences lead us to postulate that the conversion of ovalbumin to S‐ovalbumin
Saima Kint, Yoshio Tomimatsu
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Reduction of allergenicity of irradiated ovalbumin in ovalbumin-allergic mice
Radiation Physics and Chemistry, 2007Abstract Egg allergy is one of the most serious of the immediate hypersensitivity reactions to foods. Such an allergic disorder is mediated by IgE antibodies stimulated by T-helper type 2 (Th2) lymphocytes. This study was undertaken to evaluate changes of allergenicity and cytokine profiles by exposure of irradiated ovalbumin (OVA), a major allergen ...
Ji-Hyun Seo +6 more
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Sequence of chicken ovalbumin mRNA
Nature, 1978The complete sequence of chicken ovalbumin mRNA is presented; it is 1,859 residues long, excluding its terminal 'cap' and poly(A). The region coding for ovalbumin lies close to the 'cap' but is separated from the poly(A) by an extensive 3' noncoding region of 637 nucleotides which may have no function that is precisely dependent on its sequence.
L, McReynolds +7 more
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DYE‐SENSITIZED PHOTOÖXIDATION OF OVALBUMIN*
Photochemistry and Photobiology, 1966Abstract— The dye‐sensitized photodegradation of ovalbumin is shown to involve the reduction of light‐excited dye molecules by the substrate. The photodynamic denaturation of ovalbumin, therefore, results both from attack by ‘dye‐peroxide’ molecules (as is the case when the substrate can not act as a photoreductant) and from attack by OH radicals which
J S, Bellin, G, Entner
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The sulfhydryl groups of ovalbumin
Archives of Biochemistry and Biophysics, 1951Abstract 1. 1. The reactivity of the sulfhydryl groups of ovalbumin has been investigated by iodine oxidation studies and by a titrimetric method with p-chloromercuribenzoate. The titrimetric method involved the addition of p-chloromercuribenzoate to solutions of the protein buffered at pH 5.3 and back titration of the excess or unreacted mercury
L R, MacDONNELL, R B, SILVA, R E, FEENEY
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