| Literature DB >> 15996789 |
Inger Brandt1, Kris De Vriendt, Bart Devreese, Jozef Van Beeumen, Walter Van Dongen, Koen Augustyns, Ingrid De Meester, Simon Scharpé, Anne-Marie Lambeir.
Abstract
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.Entities:
Mesh：
Substances：
Year: 2005 PMID： 15996789 DOI： 10.1016/j.peptides.2005.05.016
Source DB: PubMed Journal: Peptides ISSN： 0196-9781 Impact factor: 3.750