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Isolation and characterization of α‐endorphin and γ‐endorphin from single human pituitary glands
Author(s) -
Burbach J.Peter H.,
Wiegant Victor M.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80093-9
Subject(s) - sephadex , radioimmunoassay , endorphins , size exclusion chromatography , chemistry , anterior pituitary , peptide , pituitary gland , chromatography , biochemistry , amino acid , fractionation , microbiology and biotechnology , biology , endocrinology , hormone , enzyme
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 NH 2 ‐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.