Titlebook: Inhibin, Activin and Follistatin; Regulatory Functions Toshihiro Aono (Professor and Chairman),Hiromu Sug Book 1997 Springer Science+Busine

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Expression of Inhibin Subunits, Follistatin, and Activin Receptors in Normal Testicular Cells and Teone (FSH) from the pituitary gland (1). It consists of an .-subunit, which is covalently linked by a disulfide bond to either of two .-subunits, .. or .., giving rise to inhibin A and B, respectively. Alternatively, .-subunits can dimerize to form activins: homodimers of ..- ..-subunits are designat

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Inhibin, Activin, and Follistatin: Observations on Their Role in the Physiology of Pregnancyr these subtances that range well beyond their ability to suppress or stimulate follicle-stimulating hormone (FSH) secretion. Using radioimmunoassays that have now been shown to detect not only dimeric inhibin but products of the α-subunit, changes in inhibin secretion have been identified in a vari

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Modicum

Two-Site Immunoassay for Native Inhibin Aes: .. and ... The α-subunit binds to either a ..-subunit to form inhibin A or to a ..-subunit to form inhibin B. Details of the structure of inhibin emerged after the cloning of the genes that control the production of the inhibin subunits. Separate genes code for the precursors to the α-, ..-, and

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Ultrasensitive Enzyme Immunoassays for Inhibins and Activinsassay was unable to discriminate between dimeric bioactive inhibin forms and various forms of the free alpha subunit that occur in large amounts in body fluids (3). It became popular in publications to refer to the material measurable by the Monash assay as “immunoreactive” inhibin to acknowledge th

LAVA

Immunoassays for Activin and Follistatin: Results in Normal and Diseased Subjectsecretion from the pituitary (1). Activin is a 25-kDa homodimeric protein composed of the two .-subunits of INH linked by interchain disulfide bonds, and it comprises three different forms (...., ...., and ....). Follistatin (FS) is a monomeric glycosylated protein isolated from ovarian follicular fl

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Circulating Inhibinteolytic processing sites via a series of intermediates into biologically active mature forms. Many of these potential precursors have now been isolated from follicular fluid or identified in transfected cell culture medium and cell lysates. However, the forms present in the circulation responsible

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