Combining solid-phase preconcentration, capillary electrophoresis and off-line matrix-assisted laser desorption/ionization mass spectrometry: intracerebral metabolic processing of peptide E in vivo.

Zhang H, Stoeckli M, Andren PE, Caprioli RM
J Mass Spectrom. 1999 34 (4): 377-83

PMID: 10226364 · DOI:10.1002/(SICI)1096-9888(199904)34:4<377::AID-JMS778>3.0.CO;2-D

The in vivo metabolism of peptide E was studied in the anesthetized rat using a combination of microdialysis sampling, solid-phase preconcentration capillary electrophoresis and imaging matrix-assisted laser desorption/ionization mass spectrometry (MALDI/MS). The metabolic profile of peptides identified by MALDI/MS showed that the primary enzymatic activity for degradation of peptide E was due to carboxypeptidases and, to a lesser extent, aminopeptidases and some trypsin-like endopeptidases. Over 75 metabolic fragments were detected from the action of these enzymes in vivo.

MeSH Terms (7)

Amino Acid Sequence Animals Electrophoresis, Capillary Enkephalins Mass Spectrometry Molecular Sequence Data Rats

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