ISOLATION AND CHARACTERIZATION OF FIN WHALE PROLACTIN*
A highly purified prolactin preparation has been obtained from fin whale pituitaries by extraction with acid acetone, salt precipitation, isoelectric fractionation, and exclusion chromatography on Sephadex G‐100 and ion‐exchange chromatography on DEAE‐cellulose. Fin whale prolactin was isolated in a...
Published in: | International Journal of Peptide and Protein Research |
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Main Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
1979
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Subjects: | |
Online Access: | http://dx.doi.org/10.1111/j.1399-3011.1979.tb01873.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1399-3011.1979.tb01873.x https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3011.1979.tb01873.x |
Summary: | A highly purified prolactin preparation has been obtained from fin whale pituitaries by extraction with acid acetone, salt precipitation, isoelectric fractionation, and exclusion chromatography on Sephadex G‐100 and ion‐exchange chromatography on DEAE‐cellulose. Fin whale prolactin was isolated in a yield of 250 mg/kg wet weight tissue. It was found to have a molecular weight (SDS disc gel electrophoresis) of 23,600 daltons and an α‐helix content (circular dichroism) of 50%. The amino acid composition and circular dichroism spectra were very similar to those of porcine prolactin. The partial amino acid sequence has been determined by the method of fluorescein‐isothiocyanate. Fin whale prolactin was found to be 80% as potent as ovine prolactin with regard to pigeon crop‐sac assay. |
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