PMID: 7542324Jan 1, 1995Paper

Identification by gas chromatography-mass spectrometry of an adduct between pure pig plasma benzylamine oxidase and the inhibitor 3,5-diethoxy-4-aminomethylpyridine

Journal of Enzyme Inhibition
F BuffoniV Bertini

Abstract

3,5-Diethoxy-4-aminomethylpyridine (B24) interacts with pure pig plasma benzylamine oxidase (BAO), giving a Schiff base with the carbonyl active site. This Schiff base was reduced, isolated by chemical hydrolysis of the enzyme, purified by HPLC and identified by gas chromatography-mass spectrometry (GC-MS) after derivatization. The isolated B24 adduct had the same absorption spectrum, retention time on HPLC and GC and the same mass spectrum as B24-pyridoxamine. B24, which is a reversible enzyme inhibitor, is also a weak substrate and competes with benzylamine, which is the best substrate, for the active site. These results further indicate the presence of pyridoxal-phosphate covalently linked to the pig plasma benzylamine oxidase and involved in the active site of this enzyme.

References

Feb 1, 1975·The Biochemical Journal·F Buffoni, G Ignesti
May 15, 1990·Analytical Biochemistry·F Buffoni, S Cambi
Aug 1, 1990·Biochimica Et Biophysica Acta·F Buffoni
Apr 1, 1981·Agents and Actions·F Buffoni, L Raimondi
Dec 15, 1964·Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character·F BUFFONI, H BLASCHKO

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Citations

Jan 4, 2001·Molecular Genetics and Metabolism·F Buffoni, G Ignesti
Mar 24, 2004·Inflammopharmacology·F Buffoni, G Ignesti
Oct 1, 1996·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·M PulitiF Buffoni

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