ISOLATION AND AMINO-ACID-SEQUENCE OF THE TRH-POTENTIATING PEPTIDE FROM BOVINE HYPOTHALAMUS

被引:10
作者
BULANT, M
LADRAM, A
MONTAGNE, JJ
DELFOUR, A
NICOLAS, P
机构
[1] Laboratoire de Bioactivation des Peptides, Institut Jacques Monod, Université Paris 7, 75251 Paris Cedex 05
关键词
D O I
10.1016/0006-291X(92)92319-S
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A neuropeptide termed TRH-potentiating peptide, which potentiates TRH-evoked thyrotropin secretion by antehypophysis in vitro, was isolated from an acetonic powder of bovine hypothalamus. The peptide was purified to homogeneity by a 3-step protocol involving molecular sieve filtration, ion-exchange chromatography and reverse phase high performance liquid chromatography. The complete amino acid sequence of the decapeptide was determined as Ser-Phe-Pro-Trp-Met-Glu-Ser-Asp-Val-Thr by automated Edman degradation with a solid-phase sequencer. Bovine TRH-potentiating peptide is structurally identical to Ps4, a decapeptide which was deduced from the cDNA encoding the rat TRH precursor. This study provides for the first time a direct chemical evidence for the existence of non-TRH peptides originating from posttranslational processing of the TRH precursor in vivo. © 1992.
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页码:1110 / 1118
页数:9
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