We have only a partial knowledge of fish thyrotropins (TSH) and no data about peptide sequence are available. Various HPLC techniques allowed us to purify a 31.4 kDa, heterodimeric protein from saline eel pituitary extracts containing TSH activity. Partial N-terminal sequence (24 amino acids) from one subunit was strictly identical to that of eel gonadotropin II (GTH II) alpha subunit. With regard to the second subunit, 41% of the 22 amino acids identified at the N-terminus were homologous to those of bovine beta TSH and 36% were homologous to those of eel beta GTH II. Thus, the purified protein exhibits biochemical characteristics similar to those of mammalian TSH, in particular an alpha subunit common with GTH.
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