Open AccessThe carbohydrates of the isoforms of three avian riboflavin‐binding proteins
Author(s) -
Amoresano Angela,
Brancaccio Anna,
Andolfo Annapaola,
Perduca Massimiliano,
Monaco Hugo L.,
Marino Gennaro
Publication year - 1999
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1999.00570.x
Subject(s) - quail , yolk , gene isoform , glycosylation , biochemistry , egg white , carbohydrate , isoelectric focusing , isoelectric point , mannose , biology , chemistry , enzyme , gene , food science , endocrinology
The carbohydrate chains of nine isoforms of chicken egg‐white riboflavin‐binding protein (RfBP) and six isoforms each of quail egg‐white and yolk RfBP have been structurally characterized. The two N‐glycosylation sites, Asn36 and Asn147, of the most abundant isoform of each of the three proteins were analyzed in further detail leading to the identification of different glycosylation patterns. In both chicken and quail egg‐white RfBP the carbohydrates attached to position 36 had a lower degree of branching and, in the case of the quail protein, this site was only partially glycosylated. A very heterogeneous mixture of complex structures was characteristic of the other glycosylation site. Analysis of the two sites in quail yolk RfBP confirmed this result which agrees with what has been established for hen yolk RfBP. The presence in the three proteins of a highly heterogeneous mixture of differently branched glycans suggests that the differences in isoelectric points, which is a peculiarity of the different isoforms, are probably indeed due to differences in carbohydrate structure.