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. 1971 Feb;121(3):537–547. doi: 10.1042/bj1210537

Studies on the composition of egg-white ovomucin

D S Robinson 1, J B Monsey 1
PMCID: PMC1176603  PMID: 5119791

Abstract

1. Purified ovomucin was isolated as an insoluble glycoprotein complex from thick egg white. 2. A homogeneous glycoprotein, designated α-ovomucin, of molecular weight 210000 and containing N-acetylglucosamine (6.7%, w/w), N-acetylgalactosamine (0.6%, w/w), galactose (1.8%, w/w), mannose (4.6%, w/w), N-acetylneuraminic acid (1.0%, w/w) and sulphate (0.7%, w/w), was isolated from preparations of reduced ovomucin by sedimentation equilibrium in a density gradient of caesium chloride formed in the presence of 4m-guanidine hydrochloride. 3. A carbohydrate-rich fraction, designated β-ovomucin (which is homogeneous by sedimentation-velocity analysis in 5m-guanidine hydrochloride but which is heterogeneous by analytical sedimentation equilibrium in a density gradient of caesium chloride in the presence of 4m-guanidine hydrochloride), containing N-acetylglucosamine (11.0%, w/w), N-acetylgalactosamine (8.7%, w/w), galactose (19.2%, w/w), mannose (4.1%, w/w), N-acetylneuraminic acid (13.8%, w/w) and sulphate (2.7%, w/w), was also obtained from preparations of reduced ovomucin by the density-gradient method. 4. Mild acid hydrolysis of the unfractionated ovomucin complex showed that N-acetylneuraminic acid occupied a terminal position of the oligosaccharide chains. 5. Alkaline β-elimination reactions with the unfractionated ovomucin complex indicated that N-acetylgalactosamine was linked by alkali-labile bonds to hydroxy amino acids.

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Selected References

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