Changes in Glycosylation Alter the Affinity of the Human Transferrin for Its Placental Receptor.
By using serial lectin-Sepharose affinity chromatography (ConA, DSA, and LCA), the transferrins carrying the biantennary complex type of oligosaccharides from sera of healthy individuals and those carrying multiantennary oligosaccharides from sera of pregnant women were purified. The two kinds of transferrins were used to study their binding affinity for isolated placental transferring receptor. The results showed that the binding affinity of the highly branched transferring decreased to half of that for the biantennary type with a K(d) of 9.80x10(-8) M as against the latter's 4.97x10(-8) M while the maximum binding remains constant. These results suggested that changes in glycosylation altered the affinity of the human transferrin for its placental receptor.
Huang
Yong
Y
Ministry of Public Health, Key Laboratory of Glycoconjugate Research, Department of Biochemistry, Shanghai Medical University, Shanghai 200032, China.
Gu
Jian-Xin
JX