Results 321 to 330 of about 123,127 (337)

Gut Microbiota as Targets for Preventing Ovalbumin-Induced Food Allergy. [PDF]

open access: yesNutrients
Shi X   +7 more
europepmc   +1 more source

β-glucan induced trained immunity enhances antibody levels in a vaccination model in mice. [PDF]

open access: yesPLoS One
Ajit J   +7 more
europepmc   +1 more source
Some of the next articles are maybe not open access.

Related searches:

Thermostability of Refolded Ovalbumin andS-Ovalbumin

Bioscience, Biotechnology, and Biochemistry, 2005
Ovalbumin, 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 ...
Masaaki Hirose   +5 more
openaire   +3 more sources

Biosynthesis of Ovalbumin

Nature, 1959
THE problem of the biosynthesis of ovalbumin is interesting since this protein seems to be synthesized from a non-homogeneous pool of intermediary peptides1–3. We have studied the biosynthesis of this protein in vivo by the laying hen using L-cystine-35S and Na2 14CO3. Selected birds were given these labelled substances and blood was obtained at stated
D. V. Siva Sankar   +2 more
openaire   +3 more sources

The carbohydrate of ovalbumin

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 ...
Rex Montgomery, Yuan Chuan Lee
openaire   +3 more sources

A Raman difference spectroscopic investigation of ovalbumin and S‐ovalbumin

Biopolymers, 1979
AbstractRaman 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
openaire   +2 more sources

Role of the Intrachain Disulfide Bond of Ovalbumin during Conversion into S-Ovalbumin

Bioscience, Biotechnology, and Biochemistry, 1996
Disulfide-reduced and carboxymethylated ovalbumin was treated at pH 9.9 and 55 degrees C for 24 h as a specific condition for preparation of S-ovalbumin. The stability and conformation of the product were investigated. Such alkaline treatment converted native protein to S-ovalbumin, but this modified ovalbumin was not stabilized, according to results ...
Eizo Tatsumi   +3 more
openaire   +3 more sources

Structure and properties of ovalbumin

Journal of Chromatography B: Biomedical Sciences and Applications, 2001
Ovalbumin 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.
James A. Huntington, Penelope E. Stein
openaire   +3 more sources

Home - About - Disclaimer - Privacy