人胎盘中的强啡肽A（1-8）：通过串联质谱法测定的氨基酸序列

Dynorphin A(1-8) in human placenta: amino acid sequence determined by tandem mass spectrometry.

作者信息

Agbas A, Ahmed M S, Millington W, Cemerikic B, Desiderio D M, Tseng J L, Dass C

机构信息

School of Biological Sciences, Division of Molecular Biology and Biochemistry, University of Missouri, Kansas City 64108-2792, USA.

出版信息

Peptides. 1995;16(4):623-7. doi: 10.1016/0196-9781(95)00013-a.

DOI:10.1016/0196-9781(95)00013-a

PMID:7479294

Abstract

Presence of the kappa receptor-preferring neuropeptide dynorphin A(1-8) in human placenta has been demonstrated by mass spectrometry to establish rigorously the appropriate molecular weight and amino acid sequence. Liquid secondary ionization mass spectrometry produced the protonated molecule ion, (M + H)+, at m/z 981 of the endogenous peptide, and tandem mass spectrometry collected the product ion spectrum that contained the appropriate amino acid sequence-determining fragment ions produced from the precursor ion (M + H)+. The amino acid sequence of the peptide is YGGFLRRI.

摘要

通过质谱法已证实人胎盘中存在优先结合κ受体的神经肽强啡肽A(1 - 8)，以严格确定其合适的分子量和氨基酸序列。液体二次离子质谱法产生了内源性肽的质子化分子离子(M + H)+，其质荷比为981，串联质谱法收集了产物离子谱，该谱包含从前体离子(M + H)+产生的合适的氨基酸序列确定碎片离子。该肽的氨基酸序列为YGGFLRRI。