Characterization of E‐PHA‐reactive α‐fetoprotein isoforms by two‐dimensional lectin affinity electrophoresis

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Abstract
Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human α-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin. By means of neuraminidase and/or β-galactosidase treatment, AFP-P2 was identified as α2→6 disialo-AFP, AFP-P3 as having biantennary structures with α2→6 monosialylated galactose of the Mannose (Man) α1→6 arm, AFP-P4 as having α2→6 monosialylated galactose of the Man α1→3 arm, and AFP-P5 as disialo-AFP with α2→3 sialylated galactose of the Man α1→6 antenna and with α2→6 sialylated galactose of the other antenna. Desialylated AFP with the terminal galactose of the Man α1→6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man α1→6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively. Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.

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