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Please use this identifier to cite or link to this item: http://hdl.handle.net/10057/1392

Title: Expression of a novel follicle-stimulating hormone glycoform relating to fertility
Authors: Tran, T.
Bousfield, George R.
Shuai, B.
Issue Date: 25-Apr-2008
Publisher: Wichita State University. Graduate School.
Citation: Tran, T., Bousfield, G.R., and B. Shuai (2008). Expression of a novel follicle-stimulating hormone glycoform relating to fertility . In Proceedings: 4th Annual Symposium: Graduate Research and Scholarly Projects. Wichita, KS: Wichita State University, p.127-128
Series/Report no.: GRASP
v.4
Abstract: LH) and follicle-stimulating hormone (FSH), play significant roles in follicular development and maintenance of the estrous cycle. FSH specifically functions to stimulate follicle growth, estrogen synthesis and serve as a selection factor for dominant follicles, which are essential to maintain fertility. FSH exists in two glycoforms: diglycosylated FSH (DiGlycFSH) and tetraglycosylated FSH (TetGlycFSH). The DiGlycFSH contains carbohydrates on the α subunit only, while TetGlycFSH has carbohydrates on both α and β subunits. Pituitary extraction of FSH shows that in young reproductive age women, the DiGlycFSH is more abundant than TetGlycFSH, whereas post menopausal women have more pituitary TetGlycFSH. Bioassay of DiGlycFSH shows that it has greater biological activity than TetGlycFSH. Due to limited availability of DiGlycFSH, bacterial expression of recombinant human (h)FSH (rec hFSH) is needed to provide sufficient glycoform for structural and biological studies. We report our efforts towards synthesis of DiGlycFSH, which involves expression of rec hFSHβ, separation, purification from soluble and insoluble fractions, folding, and reassociation with human chorionic gonadotropin (hCGα). Protein function will be characterized by receptor binding and steroidogenesis assays.
Description: Paper presented to the 4th Annual Symposium on Graduate Research and Scholarly Projects (GRASP) held at the Hughes Metropolitan Complex, Wichita State University, April 25, 2008.
Research completed at the Department of Biological Sciences, College of Liberal Arts and Sciences
URI: http://hdl.handle.net/10057/1392
Appears in Collections:BIO Graduate Student Conference Papers
Proceedings: 4th Annual Symposium: Graduate Research and Scholarly Projects

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