Abstract
In these experiments we have studied the in vitro metabolism of LVV-hemorphin-7 in human plasma by using reversed-phase high-performance liquid chromatography (RP-HPLC) in combination with micro-electrospray mass spectrometry (micro-ES-MS). Tandem mass spectrometry (MS-MS) was performed in order to verify the structure of the peptide fragments found. Incubations were performed with and without different protease inhibitors. Results showed that LVV-hemorphin-7 was metabolized from the N-terminal end of the peptide, probably by an amastatin-sensitive exopeptidase.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Angiotensin-Converting Enzyme Inhibitors / chemistry
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Angiotensin-Converting Enzyme Inhibitors / metabolism
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Anti-Bacterial Agents / metabolism
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Captopril / metabolism
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Chromatography, High Pressure Liquid
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Endorphins / chemistry
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Gas Chromatography-Mass Spectrometry
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Glycopeptides / metabolism
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Hemoglobins / analysis*
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Hemoglobins / chemistry
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Hemoglobins / metabolism*
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Humans
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Molecular Sequence Data
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Opioid Peptides / chemistry
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Peptide Fragments / analysis*
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism*
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Peptides*
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Plasma / enzymology*
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Protease Inhibitors / metabolism
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Spectrophotometry, Ultraviolet
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Time Factors
Substances
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Angiotensin-Converting Enzyme Inhibitors
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Anti-Bacterial Agents
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Endorphins
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Glycopeptides
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Hemoglobins
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Opioid Peptides
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Peptide Fragments
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Peptides
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Protease Inhibitors
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hemorphin 6
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hemorphin 4
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hemorphin 7
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amastatin
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LVV-hemorphin-7
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Captopril
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phosphoramidon