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Biochem Biophys Res Commun. 1998 Apr 28;245(3):847-52.

High-level secretion of biologically active recombinant porcine follicle-stimulating hormone by the methylotrophic yeast Pichia pastoris.

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  • 1Unité Récepteurs et Communications Cellulaires, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.

Abstract

An active recombinant glycoprotein hormone, porcine follicle-stimulating hormone (recFSH), has been produced for the first time in the methylotrophic yeast, Pichia pastoris. The yield of secreted recFSH (10 mg/l) was the highest ever reached. RecFSH displayed an apparent molecular mass of 41 kDa by SDS-PAGE and was found to bear only N-linked carbohydrates of the high-mannose type. Its in vitro binding and cell-stimulating activities were identical to those of pituitary porcine FSH. The large availability and the noncharged N-glycans of FSHrec should render it highly valuable for structural studies.

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