Purification and properties of bullfrog prolactin

K. Yamamoto, S. Kikuyama

    Research output: Contribution to journalArticle

    53 Citations (Scopus)

    Abstract

    Prolactin was purified from bullfrog adenohypophyses by extraction of acetone-dried powder with acid acetone and chromatography on DEAE-cellulose and Sephadex G100. The bullfrog prolactin had a molecular weight of 23,000 as determined by SDS gel electrophoresis. The isoelectric point was 5.76 when determined by electrofocusing. The amino acid composition of the purified prolactin closely resembles that of mammalian prolactin. The prolactin was found to be 3.6 times as potent as bovine prolactin in promoting collagen synthesis in the tadpole tail fin.

    Original languageEnglish
    Pages (from-to)59-64
    Number of pages6
    JournalEndocrinologia Japonica
    Volume28
    Issue number1
    Publication statusPublished - 1981

    Fingerprint

    Rana catesbeiana
    Prolactin
    Acetone
    DEAE-Dextran
    Anterior Pituitary Gland
    Isoelectric Point
    Isoelectric Focusing
    Powders
    Larva
    Electrophoresis
    Tail
    Chromatography
    Collagen
    Molecular Weight
    Gels
    Amino Acids
    Acids

    ASJC Scopus subject areas

    • Endocrinology

    Cite this

    Yamamoto, K., & Kikuyama, S. (1981). Purification and properties of bullfrog prolactin. Endocrinologia Japonica, 28(1), 59-64.

    Purification and properties of bullfrog prolactin. / Yamamoto, K.; Kikuyama, S.

    In: Endocrinologia Japonica, Vol. 28, No. 1, 1981, p. 59-64.

    Research output: Contribution to journalArticle

    Yamamoto, K & Kikuyama, S 1981, 'Purification and properties of bullfrog prolactin', Endocrinologia Japonica, vol. 28, no. 1, pp. 59-64.
    Yamamoto, K. ; Kikuyama, S. / Purification and properties of bullfrog prolactin. In: Endocrinologia Japonica. 1981 ; Vol. 28, No. 1. pp. 59-64.
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