Structural studies on periodate-oxidized chicken ovomucoid. Spectral behaviour of the tyrosine residues.
About 50% of the carbohydrate moiety of ovomucoid was destroyed by periodate oxidation. The oxidation was carried out for 6 h or 24 h. The data obtained showed that in the carbohydrate chain 2-5 glucosamines and 1-2 neutral sugar residues were decomposed with the consumption of 16 mol and 29 mol of periodate respectively. Periodic oxidation slightly changed the inhibitory activity of the ovomucoid, but altered its spectral properties. An increase of the absorption maximum at 278 nm was noted, as well as a tendency for normalization of phenolic ionization and an increase of the relative fluorescence. The reactivity of tyrosine residues towards tetranitromethane is also changed. It was suggested that even in native ovomucoid the tyrosines could be regarded as 'dissolved' in the 'carbohydrate solvent'. This contact could be achieved by the hydrogen bonds in the formation of which the NHCOCH3 groups of the glucosamine residues play an essential role. Peroxidate oxidation seems to lead to an alteration of the nature of the 'sugar solvent' and disturbs the conformation of the sugar chain.
D000117:Acetylglucosamine / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D004527:Egg Proteins; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D010059:Ovomucin; D010084:Oxidation-Reduction; D010504:Periodic Acid; D010636:Phenols; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013774:Tetranitromethane; D014443:Tyrosine / Q000032:analysis
D000596:Amino Acids; D004527:Egg Proteins; D010636:Phenols; D010504:Periodic Acid; D010059:Ovomucin; D014443:Tyrosine; D013774:Tetranitromethane; D000117:Acetylglucosamine