Studies on Egg White Protein
نویسندگان
چکیده
منابع مشابه
Amino acid sequence studies on bobwhite quail egg white lysozyme.
To test the immunological prediction that there should be two amino acid sequence differences between the lysozymes of the bobwhite quail and the chicken, the sequences of these two lysozymes have now been compared. Lysozyme purified from bobwhite quail egg white was reduced, carboxymethylated, and digested with trypsin. The resulting 18 peptides were separated and their compositions determined...
متن کاملOvoglycoprotein, a protein of hen's-egg white.
1. A description is given of the isolation of a glycoprotein from hen's-egg white; it has been called ovoglycoprotein. 2. It contains 13.6% of hexose, 13.8% of hexosamine and 3% of sialic acid. 3. Hexose occurs as mannose and galactose in the ratio 2:1, hexosamine as glucosamine and sialic acid as N-acetylneuraminic acid. 4. It has S(20,w) 2.47s and a minimum molecular weight, calculated from t...
متن کاملNative and denatured egg white protein IgE tests discriminate hen's egg allergic from egg-tolerant children.
BACKGROUND Accurate diagnosis of egg allergy by IgE testing is challenged by a large number of atopic subjects sensitized, but clinically tolerant to eggs. In addition, discrimination between allergy to raw only, or raw and cooked egg allergy is important. In this study, we investigate the diagnostic performance of IgE tests to native and denatured egg proteins. METHODS According to food chal...
متن کاملBiotin-binding protein from egg yolk. A protein distinct from egg white avidin.
Biotin-binding protein has been purified 2000-fold from chicken egg yolk with a 1 to 2% yield. The puriflcation includes l-butanol extraction of yolk lipids, phosphocellulose chromatography of water-soluble proteins, affinity binding and elution from biotinylSepharose, and gel filtration chromatography. Since the protein biotin-binding sites are saturated with very tightly bound biotin, a novel...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1969
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.33.75