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Isolation and characterization of turkey prolactin

Summary. Prolactin from frozen turkey pituitary glands was purified by alkaline ethanol extraction of the pituitary residue after pre-extractions of the gonadotrophins and GH, followed by gel filtration on Sephadex G-100 and DEAE—cellulose column chromatography at different pH. A specific radioligand—receptor assay for ovine prolactin was used to locate the activity in eluates after column chromatography and gel filtration. The potency of the highly purified turkey prolactin was characterized by a radioligand—receptor assay to be 3·40 i.u./mg and by a heterologous radioimmunoassay to be 35 i.u./mg as compared to purified ovine prolactin as standard. The yield of turkey prolactin was 3 mg/100 g frozen pituitary glands. The purified turkey prolactin consisted of three protein bands upon polyacrylamide gel electrophoresis and the molecular weight was estimated to be 22 000 by SDS-polyacrylamide gel electrophoresis. Turkey prolactin was rich in aspartic acid, glutamic acid and leucine, but lacking in methionine.