Search for substrates for prolyl oligopeptidase in porcine brain

被引：34

作者：

Brandt, I

De Vriendt, K

Devreese, B

Van Beeumen, J

Van Dongen, W

Augustyns, K

De Meester, I

Scharpé, S

Lambeir, AM

机构：

[1] Univ Instelling Antwerp, Dept Pharmaceut Sci, Med Biochem Lab, B-2610 Antwerp, Belgium

[2] Univ Ghent, Lab Prot Biochem & Prot Engn, B-9000 Ghent, Belgium

[3] Univ Antwerp, Ctr Mass Spectrometry & Proteome Anal, B-2020 Antwerp, Belgium

[4] Univ Instelling Antwerp, Med Chem Lab, B-2610 Antwerp, Belgium

来源：

PEPTIDES | 2005年 / 26卷 / 12期

关键词：

prolyl oligopeptidase; brain; peptidomics; 2D chromatography; mass spectrometry;

D O I：

10.1016/j.peptides.2005.05.016

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：

The function of prolyl oligopeptidase (PO) has been associated with several disorders of the central nervous system. The purpose of this study was to identify endogenous substrates for recombinant porcine PO in porcine brain. The smaller polypeptides were extracted from total brain homogenates and fractionated by two-dimensional chromatography prior to incubation with PO. Shifts in the mass spectrum between the control and the incubated sample, marked potential substrates. Using MSMS peptide sequencing techniques, we identified several fragments of intracellular proteins as potential substrates, which opens new perspectives for finding the function of PO in the intracellular space. (c) 2005 Elsevier Inc. All rights reserved.

引用

页码：2536 / 2546

页数：11

共 45 条

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