Abstract
Inhibin is a glycoprotein consisting of two dissimilar subunits, termed α and β, that are linked by disulfide bonds (1–4). There are two β-subunit types: β A and β B. The α-subunit binds to either a β A-subunit to form inhibin A or to a β B-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-, β A-, and β B-subunits, and these proteins are subsequently cleaved at sites of paired basic amino acids to yield the 20-kDa α-subunit and the 15-kDa β-subunits (5–9). Activin is a β-subunit dimer and consists of inhibin β A- and β B-subunits that have been termed activin A, activin AB, and activin B (10–12).
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Hasegawa, Y. et al. (1997). Two-Site Immunoassay for Native Inhibin A. 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_10
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DOI: https://doi.org/10.1007/978-1-4612-1874-6_10
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