CHARACTERIZATION OF GLYCOPROTEIN FRACTION FROM CARP PITUITARIES ISOLATED USING CONCANAVALIN-A AS THE AFFINITY LIGAND

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) corr esponding to the carp gonadotropin cGtH II was composed of two subunit s as determined using SDS-PAGE. This protein fraction was further divi ded into four components using reversed-phase HPLC. Two fractions were pure alpha and beta subunits of cGtH II as follows from immunodetecti on and from determination of N-terminal amino acid sequences. The othe r two were a mixture of alpha and beta subunits as was also revealed b y N-terminal analysis. Capillary electrophoresis was also used for cha racterization of isolated glycoproteins.