Isolation and characterization of α‐endorphin and γ‐endorphin from single human pituitary glands

FEBS Letters

Burbach, J.Peter H.¹  Wiegant, Victor M.¹ 

[1] Rudolf Magnus Institute for Pharmacology, Medical Faculty, University of Utrecht, Vondellaan 6, 3521 GD Utrecht, The Netherlands

关键词: α-Endorphin;    γ-Endorphin;    Human pituitary gland;    β-Endorphin fragment;    Peptide isolation;   

DOI  :  10.1016/0014-5793(84)80093-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α-endorphin and γ-endorphin, two closely related peptides of the pro-opiomelanocortin family with characteristics biological activities, were purified to homogeneity from single human pituitary glands and chemically identified. Isolation of the peptides was based on size fractionation by Sephadex G-75 chromatography followed by two HPLC steps using reverse-phase and paired-ion reverse-phase systems and was monitored by radioimmunoassay. During the isolation procedure α-and γ-endorphin-sized material behaved chromatographically and immunologically indistinguishably from synthetic α- and γ- endorphin. The amino acid composition and NH₂-terminus of isolated peptides demonstrated their identity as authentic α-endorphin and γ-endorphin. Acetylated forms were absent. In addition, evidence is provided that large forms with α- and γ-endorphin immunoreactivity detected during gel filtration are human lipotropin-(1–74) and -(1–75), respectively. The data substantiate that α-endorphin and γ-endorphin exist as endogenous peptides in the human pituitary gland.

【 授权许可】

Unknown