Abstract
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 NH 2-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.
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