Gel high-performance liquid chromatographic studies on the elution behavior of chemically deglycosylated human chorionic gonadotropin and its subunits.
The elution behavior of human chorionic gonadotropin and its subunits, and their desialylated and deglycosylated derivatives was studied on gel high-performance liquid chromatography. Using three TSK G-SW columns, excellent separations were achieved for eleven human chorionic gonadotropin derivatives. In a comparison of the native (30% carbohydrate content), asialo (24%) and HF-deglycosylated (8%) subunits, the estimated values of molecular weights on the basis of a series of reference globular proteins deviated in various degrees from the actual molecular weight. The extent of deviation depended on the carbohydrate content and possibly the location of carbohydrate chains. The data from recombination studies suggest that the beta-subunit is the dominant determinant for their expanded molecular size.
D006063:Chorionic Gonadotropin / Q000032:analysis / Q000302:isolation & purification*; D018997:Chorionic Gonadotropin, beta Subunit, Human; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D015292:Glycoprotein Hormones, alpha Subunit; D006801:Humans; D008970:Molecular Weight; D009439:Neuraminidase; D010446:Peptide Fragments / Q000032:analysis
D006063:Chorionic Gonadotropin; D018997:Chorionic Gonadotropin, beta Subunit, Human; D015292:Glycoprotein Hormones, alpha Subunit; C034923:HCG, deglycosylated; D010446:Peptide Fragments; D009439:Neuraminidase