The mammalian form of gonadotropin-releasing hormone (GnRH) was purifi
ed from the brains of Russian sturgeon, Acipenser gueldenstaedti, usin
g reversed-phase high pressure liquid chromatography (HPLC). The total
concentration of mGnRH within these fish was 5.4 ng/brain. Small amou
nts of immunoreactive chicken GnRH-II like molecules were also detecte
d but at insufficient quantities for purification, The primary structu
re of mGnRH was determined using automated Edman degradation. Because
sequence data could not be obtained until after digestion by bovine py
roglutamyl aminopeptidase, it was determined that the amino-terminal r
esidue was modified. Furthermore, mass spectrometric data and co-eluti
on with synthetic mGnRH on HPLC confirmed that the carboxy-terminal re
sidue was amidated. The amino acid sequence of sturgeon GnRH is pGlu-H
is-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.