In vitro processing of the artificial analog of beta-lipotropin

The processing of the recombinant analogue of beta-lipotropin (beta-LHP) having 11 additional N-terminal amino acid residues and separated from the hormone by the processing signal, was investigated using rat adrenal secretory granule lysate as a test system of processing "in vitro". It wa...

Full description

Saved in:
Bibliographic Details
Published inBiokhimiia (Moscow, Russia) Vol. 55; no. 5; p. 848
Main Authors Kuz'menko, A P, Fedosov, S A, Golovin, S Ia, Mamaev, L V, Korzhov, V A, Il'ichev, A A, Zagrebel'nyĭ, S N
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.05.1990
Subjects
Adrenal Medulla - metabolism
Amino Acid Sequence
Animals
beta-Endorphin - analysis
beta-Lipotropin - biosynthesis
beta-Lipotropin - genetics
Cattle
Cytoplasmic Granules - metabolism
Humans
Hydrolysis
Molecular Sequence Data
Plasmids
Rats
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Online AccessGet more information

Cover

More Information
Summary:The processing of the recombinant analogue of beta-lipotropin (beta-LHP) having 11 additional N-terminal amino acid residues and separated from the hormone by the processing signal, was investigated using rat adrenal secretory granule lysate as a test system of processing "in vitro". It was found that incubation of the beta-LPH analogue with secretory granule enzymes leads to its limited specific degradation with a release of native beta-endorphin. It is concluded that the additional N-terminal amino acids induced no qualitative changes in beta-LPH processing.
ISSN:0320-9725