Purification and characterization of Atlantic salmon prolactin

O Andersen; V Skibeli; K M Gautvik

doi:10.1016/0016-6480(89)90191-3

Purification and characterization of Atlantic salmon prolactin

Gen Comp Endocrinol. 1989 Mar;73(3):354-60. doi: 10.1016/0016-6480(89)90191-3.

Authors

O Andersen¹, V Skibeli, K M Gautvik

Affiliation

¹ Institute of Medical Biochemistry, University of Oslo, Norway.

PMID: 2925076
DOI: 10.1016/0016-6480(89)90191-3

Abstract

Prolactin was isolated from the Atlantic salmon (Salmo salar) pituitary gland by extraction with acid acetone, gel filtration, ion exchange-chromatography, and reversed-phase high-performance liquid chromatography. The yield was 0.6 mg/g wet tissue. The hormone had a molecular weight of 23.5 kDa as determined by SDS-polyacrylamide gel electrophoresis. Isoelectric focusing gave an isoelectric point of 9.2. The N-terminal sequence and the amino acid composition indicated extensive homology between Atlantic and Pacific salmon prolactin. Antiserum against Atlantic salmon prolactin cross-reacted with chum salmon prolactin, but not with human, rat, or sheep prolactin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amino Acids / analysis
Animals
Female
Male
Molecular Sequence Data
Pituitary Gland, Anterior / analysis*
Prolactin / analysis
Prolactin / isolation & purification*
Salmon / physiology*

Substances

Amino Acids
Prolactin