Abstract
Background Human follicle stimulating hormone (hFSH), synthesized by the human pituitary gland, is a biologically active glycoprotein composed of two noncovalently bound αand βsubunits and is critically involved in the maturation of ovarian follicles and in spermatogenesis. Considerable heterogeneity associated with different hFSH preparations has been reported, mainly related to the presence of different glycoforms [1]. The characterization of preparations of hFSH utilized as a therapeutic agent in reproductive medicine is therefore very important, especially considering that no specific monography has yet been published by the main pharmacopoeias.
Highlights
Human follicle stimulating hormone, synthesized by the human pituitary gland, is a biologically active glycoprotein composed of two noncovalently bound α- and β- subunits and is critically involved in the maturation of ovarian follicles and in spermatogenesis
Studies were conducted to assess and compare hydrophobicity, molecular weight, charge heterogeneity and purity of the natural and recombinant heterodimeric preparations. These characteristics were examined by reversed-phase high performance liquid chromatography (RP-HPLC), matrixassisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF), isoelectric focusing and sizeexclusion high performance liquid chromatography (HPSEC)
Urinary-derived Human follicle stimulating hormone (hFSH) presented the lowest HPSEC tR, in agreement with the highest molecular mass more accurately determined by MALDI-TOF mass spectrometry
Summary
Human follicle stimulating hormone (hFSH), synthesized by the human pituitary gland, is a biologically active glycoprotein composed of two noncovalently bound α- and β- subunits and is critically involved in the maturation of ovarian follicles and in spermatogenesis. Analysis and characterization of different preparations of recombinant human follicle stimulating hormone (hFSH) and of its subunits In this work four hFSH preparations were analyzed, two of them being natural (pituitary- and urinary-derived) and the other two recombinant (CHO-derived).
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