C‐terminal amidation of neuropeptides

FEBS Letters

Cohen, Paul²  Fromageot, Pierre¹  Morgat, Jean-Louis¹  Hung, Lam Than¹  Gomez, Sophie²  Genet, Roger¹  di Bello, Carlo³ 

[1] Service de Biochimie, Departement de Biologie, CEN Saclay, 91191 Gif-sur-Yvette, France;Groupe de Neurobiochimie Cellulaire et Moléculaire, Université Pierre et Marie Curie, 96 boulevard Raspail, 75006, Paris, France;Istituto di Chimica Biologica, Università di Padova, 35100 Padova, Italy

关键词: Thyroliberin;    Hypothalamic granule;    TRH-Gly;    TRH-Gly-Lys-Arg;    TRH;    pGlu-His-Pro(NH2) (thyroliberin);    TRH-Gly;    pGlu-His-Pro-Gly;    TLC;    thin-layer chromatography;    HPLC;    high-performance liquid chromatography;    CMC;    carboxymethylcellulose;    CRF;    corticotropin releasing factor;   

DOI  :  10.1016/0014-5793(84)80853-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Biosynthesis of the C-terminal carboxamide group of peptide hormones was studied using comparatively pGlu-His-Pro-Gly and Glu-His-Pro-Gly-Lys-Arg as putative precursors of the tripeptide, thyroliberin (TRH). Rat hypothalamus granules were found to contain an amide group forming activity which converts both peptide substrates into TRH. Comparison of the rate of conversion of the two substrates indicated that the C-terminal dibasic extension favored a 10-fold increase in the production of amidated peptide. It is suggested that this type of structure may be present in the putative biosynthetic precursor of TRH and that it may provide a better substrate for the enzyme(s) involved in C-terminal amidation.

【 授权许可】

Unknown