Open AccessIn vitro biosynthesis of beta-endorphin in pituitary glands.
Author(s) -
Philippe Crine,
Suzanne Benjannet,
Nabil G. Seidah,
M. Lis,
Michel Chrétien
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.4.1403
Subject(s) - pituitary gland , methionine , endorphins , residue (chemistry) , amino acid , biosynthesis , in vitro , biochemistry , chemistry , beta endorphin , peptide , beta (programming language) , biology , stereochemistry , medicine , endocrinology , hormone , enzyme , computer science , programming language
beta-Endorphin is a 31 amino acid polypeptide isolated from the pituitary gland of different species of animals. It has strong morphine-like activity. It is formed of amino acid residues 61-91 of beta-lipotropin. Speculation has arisen whether it is biosynthesized in situ or transformed after secretion of beta-lipotropin. The present in vitro studies show that it is found as beta-endorphin in bovine pituitary slices incubated with radioactive amino acid precursor [35S]methionine. Chemical characterization and microsequencing of the newly biosynthesized material proves its identity with isolated unlabeled beta-endorphin and shows that it has a methionine residue at its fifth position, as expected.