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Endocrinology, Vol 108, 850-854, Copyright © 1981 by Endocrine Society

ARTICLES

Isolation and partial characterization of secreted hamster pituitary prolactin

P Colosi, E Markoff, A Levy, L Ogren, N Shine and F Talamantes

PRL secreted by hamster anterior pituitaries was purified by gel filtration on Sephadex G-100 and ion exchange chromatography on DEAE- cellulose. Hamster PRL eluted from Sephadex G-100 with an elution volume to void volume ratio of 1.85 and at a salt concentration of 0.13 M NaCl on DEAE-cellulose. Electrophoretic homogeneity of the hormone was demonstrated in several gel systems, and electrophoresis in the presence of sodium dodecyl sulfate indicated a molecular weight of 22,000 +/- 2,000. Hamster PRL did not cross-react with antiserum to mouse PRL. Hamster PRL displayed lactogenic activity in an in vitro mouse mammary gland assay. Hamster PRL displaced [125I]iodo-PRL from lactating rabbit mammary gland receptors. Thus, with respect to its exclusion properties on SEphadex G-100, its molecular weight, and its biological activity, hamster PRL closely resembles other mammalian PRLs.




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Copyright © 1981 by The Endocrine Society