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Isolation and Amino-acid Sequence of β-LPH from Sheep Pituitary Glands

Nature volume 208, pages 1093–1094 (1965)Cite this article

Abstract

SEVERAL adenohypophyseal hormones have been demonstrated to possess in vitro lipotropic activity; these include growth, adrenocorticotropic, thyrotropic, α-melanocyte-stimulating and β-melanocyte-stimulating hormones. Recently, Rudman, Astwood and their colleagues reported the preparation of Fraction H, peptides I and II, and showed these preparations to be lipotropic agents1,2. In the course of investigating a simplified procedure for the isolation of ACTH from sheep pituitary glands, we have obtained a lipotropic peptide3 which is chemically distinct from ACTH and other known adenohypophyseal hormones. In this communication, we wish to describe the isolation of another lipotropic peptide (designated as β-LPH) from sheep pituitaries. The complete amino-acid sequence of β-LPH will also be presented here.

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Authors and Affiliations

  1. Hormone Research Laboratory, University of California, Berkeley, California

    CHOH HAO LI, LIVIO BARNAFI, MICHEL CHRÉTIEN & DAVID CHUNG

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  1. CHOH HAO LI
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  2. LIVIO BARNAFI
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  3. MICHEL CHRÉTIEN
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  4. DAVID CHUNG
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HAO LI, C., BARNAFI, L., CHRÉTIEN, M. et al. Isolation and Amino-acid Sequence of β-LPH from Sheep Pituitary Glands. Nature 208, 1093–1094 (1965). https://doi.org/10.1038/2081093b0

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