Collect. Czech. Chem. Commun. 1998, 63, 434-440

Characterization of Glycoprotein Fraction from Carp Pituitaries Isolated Using Concanavalin A as the Affinity Ligand

Irena Hulováa,b, Jana Barthováb, Helena Ryšlaváb and Václav Kašičkaa

a Institute of Organic Chemistry and Biochemistry, 166 10 Prague 6, Czech Republic
b Department of Biochemistry, Faculty of Science, Charles University, 128 40 Prague 2, Czech Republic


Glycoproteins that have affinity to Concanavalin A were isolated from the acetone-dried pituitaries of common carp (Cyprinus carpio L.). Two fractions of glycoproteins were separated using gel chromatography on Superdex 75HR. The fraction with lower molecular weight (30 000) corresponding to the carp gonadotropin cGtH II was composed of two subunits as determined using SDS-PAGE. This protein fraction was further divided into four components using reversed-phase HPLC. Two fractions were pure α and β subunits of cGtH II as follows from immunodetection and from determination of N-terminal amino acid sequences. The other two were a mixture of α and β subunits as was also revealed by N-terminal analysis. Capillary electrophoresis was also used for characterization of isolated glycoproteins.

Keywords: Hormones; Glycoproteins; Gonadotropins; Carp pituitary; Capillary electrophoresis.