Two-Site Immunoassay for Native Inhibin A

  • Yoshihisa Hasegawa
  • Hiroo Madarame
  • Sintaro Yoshida
  • Hiroyuki Kaneko
  • Yumiko Abe
  • Hideki Mizunuma
  • Yoshito Ibuki
Part of the Serono Symposia USA book series (SERONOSYMP)

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).

Keywords

Cellulose HPLC Albumin Europium Agarose 

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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Yoshihisa Hasegawa
  • Hiroo Madarame
  • Sintaro Yoshida
  • Hiroyuki Kaneko
  • Yumiko Abe
  • Hideki Mizunuma
  • Yoshito Ibuki

There are no affiliations available

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