Purification and biological characterization of chinook salmon prolactin

Patrick Prunet (1) , Louis L. Houdebine (2)

1 Laboratoire de physiologie des poissons
2 Laboratoire de Physiologie de la Lactation

Prolactin from chinook salmon pituitaries was purified by acid acetone extraction, saline precipitation, chromatofocusing, and gel filtration. This procedure allowed us to recover highly purified prolactin as demonstrated by the presence of a single NH2-terminal amino acid and a single band in sodium dodecyl sulfate gel electrophoresis. Chinook salmon prolactin appeared to be a basic protein of 22,500 molecular weight. Throughout the purification, prolactin bioactivity was followed by radioreceptor assay for lactogenic hormones. The prolactin character of the purified protein was established by its lactogenic activity in the rabbit mammary gland in vitro and its sodium-retaining activity in hypophysectomized Fundulus heteroclitus.

Mots clés: fish; chinook salmon; hormone

Domaines: Sciences du Vivant [q-bio]

Patrick Prunet, Louis L. Houdebine. Purification and biological characterization of chinook salmon prolactin. General and Comparative Endocrinology, 1984, 53, pp.49-57. ⟨10.1016/0016-6480(84)90223-5⟩. ⟨hal-02728615⟩