High-level secretion of biologically active recombinant porcine follicle-stimulating hormone by the methylotrophic yeast Pichia pastoris.
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.
Richard
F
F
Unité Récepteurs et Communications Cellulaires, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.
Robert
P
P
Remy
J J
JJ
Martinat
N
N
Bidart
J M
JM
Salesse
R
R
Combarnous
Y
Y
D000818:Animals; D015153:Blotting, Western; D016466:CHO Cells; D006224:Cricetinae; D005640:Follicle Stimulating Hormone / Q000096:biosynthesis / Q000378:metabolism*; D008970:Molecular Weight; D010843:Pichia / Q000378:metabolism*; D011962:Receptors, FSH / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D013552:Swine
D011962:Receptors, FSH; D011994:Recombinant Proteins; D005640:Follicle Stimulating Hormone