PROCESSING OF PRODYNORPHIN-DERIVED PEPTIDES IN STRIATAL EXTRACTS - IDENTIFICATION BY ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY LINKED TO SIZE-EXCLUSION CHROMATOGRAPHY

被引：49

作者：

NYLANDER, I

TANNO, K

WINTER, A

SILBERRING, J

机构：

[1] KAROLINSKA INST, DEPT CLIN NEUROSCI, DRUG DEPENDENCE RES SECT, STOCKHOLM, SWEDEN

[2] PHARMACIA BIOTECH AB, UPPSALA, SWEDEN

[3] TOHOKU COLL PHARMACEUT SCI, SENDAI, MIYAGI, JAPAN

来源：

LIFE SCIENCES | 1995年 / 57卷 / 02期

关键词：

NEUROPEPTIDES; DYNORPHINS; ENKEPHALINS; NEUROPEPTIDE PEPTIDASES; PEPTIDOHYDROLASES;

D O I：

10.1016/0024-3205(95)00253-3

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

Proteolytic processing of prodynorphin-derived peptides in rat brain was studied with the help of high performance size exclusion chromatography (SEC) connected to electrospray ionization mass spectrometry. Extracts from rat striatum were incubated with individual synthetic dynorphin peptides. Dynorphin A was the most resistant to proteolytic cleavage, converting slowly to Leu-enkephalin (0.3 pmol/min), whereas dynorphin B was processed to this pentapeptide at a 10(4)-fold higher rate. Minor cleavage was also observed between Arg(6) - Arg(7). Alphaneoendorphin was also rapidly metabolized to Leu-enkephalin (6 nmol/min) and, to a lesser extent, to Leu-enkephalinArg(6). This new strategy for studying peptidases can easily be adapted to identification of components present in body fluids.

引用

页码：123 / 129

页数：7

共 17 条

[1] MEMBRANE-BOUND ENZYMES AND THEIR ROLE IN PROCESSING OF THE DYNORPHINS AND OF THE PROENKEPHALIN OCTAPEPTIDE MET-ENKEPHALIN-ARG-GLY-LEU [J].