Abstract
Activin (ACT) and inhibin (INH) are gonadal proteins purified on the basis of bioactivity to stimulate or inhibit follicle-stimulating hormone (FSH) secretion from the pituitary (1). Activin is a 25-kDa homodimeric protein composed of the two β-subunits of INH linked by interchain disulfide bonds, and it comprises three different forms (β A β A, β A β B, and β B β B). Follistatin (FS) is a monomeric glycosylated protein isolated from ovarian follicular fluid (FF), and is now known to neutralize the action of ACT by forming a stable complex with it (2–4). Molecular cloning has revealed the presence of two FS core proteins of 288 and 315 amino acids (FS-288 and FS-315, respectively) as a result of the alternative splicing of the precursor messenger ribonucleic acid (mRNA) (5). Further work by Sugino et al. identified six molecular forms of porcine FS caused by truncation and glycosylation (6).
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Shintani, Y. et al. (1997). Immunoassays for Activin and Follistatin: Results in Normal and Diseased Subjects. In: Aono, T., Sugino, H., Vale, W.W. (eds) Inhibin, Activin and Follistatin. Serono Symposia USA. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-1874-6_12
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DOI: https://doi.org/10.1007/978-1-4612-1874-6_12
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