[Purification and characterization of presumed thyrotropic hormone subunits of a teleost fish, the eel (Anguilla anguilla)].
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.
Laboratoire de Physiologie générale et comparée du Muséum national d'Histoire naturelle, U.R.A.-C.N.R.S. n. 90, 7, Paris.
J
J
Marchelidon
J C
JC
Huet
C
C
Salmon
J C
JC
Pernollet
Y A
YA
Fontaine
D000595:Amino Acid Sequence; D000811:Anguilla / Q000033:anatomy & histology*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006065:Gonadotropins, Pituitary / Q000737:chemistry; D008969:Molecular Sequence Data; D010902:Pituitary Gland / Q000737:chemistry; D013972:Thyrotropin / Q000737:chemistry / Q000302:isolation & purification*
D006065:Gonadotropins, Pituitary; D013972:Thyrotropin
Purification et caractérisation des sous-unités présumées de l'hormone thyréotrope d'un poisson télóestéen, l'anguille (Anguilla anguilla).