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• W2000839934 abstract "An egg white glycoprotein fraction resembling ovomucoid was purified from chicken egg white by a sequential procedure involving ammonium sulfate precipitation and ion exchange chromatography on DEAE-and CM-cellulose. The resulting preparation was homogenous as indicated by polyacrylamide gel electrophoresis at several pH values (2.3, 4.3, and 9.5), isoelectric focusing, end group analysis, ultracentrifuge studies, and immunochemical analysis. The purified material had an isoelectric point of 4.8, an average molecular weight of 27,800, and contained 3 moles of galactose, 12 moles of mannose, and 29 moles of glucosamine per mole of protein. The product inhibited bovine trypsin, forming a 1 to 1 complex on a molar basis, and elicited a positive anaphylactoid response in albino rats at levels as low as 0.5 μg. Brief exposure of the purified glycoprotein to extremes in pH did not irreversibly alter the protein conformation as indicated by circular dichroism measurements, trypsin inhibition, gel electrophoresis, and immunochemical studies. The egg white glycoprotein isolated by the above procedure differs from ovomucoid prepared by a trichloroacetic acid procedure with respect to isoelectric point, carbohydrate composition, and circular dichroism spectra" @default.
• W2000839934 created "2016-06-24" @default.
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• W2000839934 date "1974-01-01" @default.
• W2000839934 modified "2023-10-16" @default.
• W2000839934 title "The physical and chemical properties of a chicken egg white glycoprotein purified by nondenaturing methodology" @default.
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• W2000839934 doi "https://doi.org/10.1016/s0003-9861(74)80004-4" @default.
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