부산대학교 도서관

The glycoprotein hormones are heterodimeric proteins that share a common α subunit and have unique β subunits that confer receptor selectivity. One member of this family, follicle-stimulating hormone (FSH), is secreted by the pituitary and is involved in the control of male and female reproduction. Herein, we describe the construction of baculoviruses for glutathione-S-transferase (GST) fusions of the human FSH (hFSH) subunits and their expression in insect cells, either alone or with the complementary non-fused FSH subunits (FSHα or FSHβ). Only the GST-BV-hFSHα monomer and the GST-BV-hFSHα/BV-hFSHβ (GST-BV-hFSH) heterodimer were efficiently secreted into the culture supernatant. The hybrid molecule, GST-BV-hFSH, was affinity purified in one step, and demonstrated activity in receptor–radioligand binding assays and in a cAMP accumulation assay. The use of GST-BV-hFSHα provides a novel and efficient method for purifying and studying members of the glycoprotein hormone family derived from the culture supernatant or subcellular fractions of the cell. [Copyright &y& Elsevier]