|Proteomic Analyses of Recombinant Human Follicle-Stimulating Hormone and Urinary-Derived Gonadotropin Preparations|
|Authors:||Yoshimitsu Kuwabara, M.D., Ph.D., Katsuya Mine, M.D., Ph.D., Akira Katayama, Ph.D., Tomoko Inagawa, M.D., Shigeo Akira, M.D., Ph.D., and Toshiyuki Takeshita, M.D., Ph.D.|
OBJECTIVE: To understand the properties of each available gonadotropin preparation, especially in terms of the differences between urinary-derived and recombinant preparations.
STUDY DESIGN: Human menopausal gonadotropin (hMG), highly purified
stimulating hormone (uFSH- HP) and recombinant FSH (rFSH) were subjected to 2-dimensional gel electrophoresis (2-DE), and protein spots were visualized by
silver-staining procedures. Major spots were analyzed by mass spectrometry.
Fluorescent-labeled preparations were also subjected to 2-DE to evaluate the quantities of FSH isohormones contained in each preparation.
RESULTS: 2-DE and mass spectrometry analyses of hMG identified many extracellular proteins as major impurities and several plasma membrane proteins including prion proteins. Both uFSH-HP and rFSH demonstrated slight impurities and showed several a and b subunit isohormones. rFSH contained higher amounts of the basic isohormones of the a subunit than uFSH-HP, whereas the predominance of the basic isohormones was less significant in the b subunit.
CONCLUSION: Proteomic analyses demonstrated the detailed protein profiles of each preparation. Differences in the quantities of a subunit isohormones may contribute to the variations in FSH activity observed between recombinant and urinary-derived FSH preparations. (J Reprod Med 2009;54: 459-466)
|Keywords:||follicle-stimulating hormone, gonadotropin preparations, isohormone, proteomic analysis, prion protein|
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