phenylethylamine/cárie dentária

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Intracellular distribution of amines taken up by rat mast cells.

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Mast cells isolated from rat peritoneal and pleural cavities were incubated in vitro with radioactively-labelled histamine (Hi), 5-hydroxytryptamine (5-HT), dopamine (DA), noradrenaline (NA), tyramine (TA), phenylethylamine (PhEA), trptamine (TrpA), ephedrine (Eph) or amphetamine (Amph). All these

Chemical rescue of a site-specific mutant of bacterial copper amine oxidase for generation of the topa quinone cofactor.

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The topa quinone (TPQ) cofactor of copper amine oxidase is produced by posttranslational modification of a specific tyrosine residue through the copper-dependent, self-catalytic process. We have site-specifically mutated three histidine residues (His431, His433, and His592) involved in binding of

Recognition properties and competitive assays of a dual dopamine/serotonin selective molecularly imprinted polymer.

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A molecularly imprinted polymer (MIP) with dual dopamine/serotonin-like binding sites (DS-MIP) was synthesized for use as a receptor model of study the drug-interaction of biological mixed receptors at a molecular level. The polymer material was produced using methacrylic acid (MAA) and acrylamide

Molecularly imprinted poly[bis(2,2'-bithienyl)methane] film with built-in molecular recognition sites for a piezoelectric microgravimetry chemosensor for selective determination of dopamine.

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A piezoelectric microgravimetry (PM) chemosensor, featuring a film of molecularly imprinted polymer (MIP) of poly[bis(2,2'-bithienyl)methane] bearing either a 3,4-dihydroxyphenyl or benzo-18-crown-6 substituent, for selective determination of dopamine was devised and tested. A Pt/quartz resonator

Structural insights into the substrate specificity of bacterial copper amine oxidase obtained by using irreversible inhibitors.

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Copper amine oxidases (CAOs) catalyse the oxidation of various aliphatic amines to the corresponding aldehydes, ammonia and hydrogen peroxide. Although CAOs from various organisms share a highly conserved active-site structure including a protein-derived cofactor, topa quinone (TPQ), their substrate

Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone.

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The crystal structures of the copper enzyme phenylethylamine oxidase from the Gram-positive bacterium Arthrobacter globiformis (AGAO) have been determined and refined for three forms of the enzyme: the holoenzyme in its active form (at 2.2 A resolution), the holoenzyme in an inactive form (at 2.8 A

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