Purification and characterization of toad prolactin

Kazutoshi Yamamoto; Tetsuya Kobayashi; Sakaé Kikuyama

doi:10.1016/0016-6480(86)90187-5

Purification and characterization of toad prolactin

Kazutoshi Yamamoto, Tetsuya Kobayashi, Sakaé Kikuyama^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

Prolactin (PRL) was purified from anterior pituitary glands of adult toad (Bufo japonicus formosus) by extraction of acetone-dried pituitary powder with acid acetone and chromatography on DEAE-cellulose and Sephadex G-100. Purification was monitored by radioimmunoassay developed for bullfrog PRL. Toad PRL thus obtained is as potent as bovine PRL in promoting collagen synthesis in the bullfrog tadpole tail fin. HPLC of the toad PRL on a reverse-phase column shows that the preparation behaves as a homogeneous protein. The hormone has a molecular weight of 23,000 as determined by SDS gel electrophoresis. The isoelectric point is 5.5 as determined by analytical electrofocusing. The amino acid composition closely resembles that of bullfrog PRL.

Original language	English
Pages (from-to)	104-109
Number of pages	6
Journal	General and Comparative Endocrinology
Volume	63
Issue number	1
DOIs	https://doi.org/10.1016/0016-6480(86)90187-5
Publication status	Published - 1986

ASJC Scopus subject areas

Endocrinology

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10.1016/0016-6480(86)90187-5

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title = "Purification and characterization of toad prolactin",

abstract = "Prolactin (PRL) was purified from anterior pituitary glands of adult toad (Bufo japonicus formosus) by extraction of acetone-dried pituitary powder with acid acetone and chromatography on DEAE-cellulose and Sephadex G-100. Purification was monitored by radioimmunoassay developed for bullfrog PRL. Toad PRL thus obtained is as potent as bovine PRL in promoting collagen synthesis in the bullfrog tadpole tail fin. HPLC of the toad PRL on a reverse-phase column shows that the preparation behaves as a homogeneous protein. The hormone has a molecular weight of 23,000 as determined by SDS gel electrophoresis. The isoelectric point is 5.5 as determined by analytical electrofocusing. The amino acid composition closely resembles that of bullfrog PRL.",

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T1 - Purification and characterization of toad prolactin

AU - Yamamoto, Kazutoshi

AU - Kobayashi, Tetsuya

AU - Kikuyama, Sakaé

PY - 1986

Y1 - 1986

N2 - Prolactin (PRL) was purified from anterior pituitary glands of adult toad (Bufo japonicus formosus) by extraction of acetone-dried pituitary powder with acid acetone and chromatography on DEAE-cellulose and Sephadex G-100. Purification was monitored by radioimmunoassay developed for bullfrog PRL. Toad PRL thus obtained is as potent as bovine PRL in promoting collagen synthesis in the bullfrog tadpole tail fin. HPLC of the toad PRL on a reverse-phase column shows that the preparation behaves as a homogeneous protein. The hormone has a molecular weight of 23,000 as determined by SDS gel electrophoresis. The isoelectric point is 5.5 as determined by analytical electrofocusing. The amino acid composition closely resembles that of bullfrog PRL.

AB - Prolactin (PRL) was purified from anterior pituitary glands of adult toad (Bufo japonicus formosus) by extraction of acetone-dried pituitary powder with acid acetone and chromatography on DEAE-cellulose and Sephadex G-100. Purification was monitored by radioimmunoassay developed for bullfrog PRL. Toad PRL thus obtained is as potent as bovine PRL in promoting collagen synthesis in the bullfrog tadpole tail fin. HPLC of the toad PRL on a reverse-phase column shows that the preparation behaves as a homogeneous protein. The hormone has a molecular weight of 23,000 as determined by SDS gel electrophoresis. The isoelectric point is 5.5 as determined by analytical electrofocusing. The amino acid composition closely resembles that of bullfrog PRL.

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Purification and characterization of toad prolactin

Abstract

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