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Investigation of amino acid changes in self-sustaining coacervates in presence of alpha-naphthyl amine and beta-naphthyl amine.

Pronounced variation of amino acids was exhibited. Phenylalanine and tryptophan were invariably present, except at very few exposure periods. Methionine was perceived in many studies in alpha-naphthylamine, while in the study of beta-naphthylamine it was observed at four days' exposure. alpha-Naphthylamine produced cysteine along with tyrosine, leucine, isoleucine, and norleucine, while beta-naphthylamine gave valine along with tyrosine, leucine, isoleucine, and norleucine. Complete variation from blank signifies the effect of alpha- and beta-naphthyl amine on the mixture.

1-Naphthylamine↗

Selective dehydrogenation of amines with respect to coordination geometry: different oxidation products of tricyano[bis(2-pyridylmethyl)amine]ferrate(II) between mer- and fac-isomers.

Both the fac- and mer-isomers of tricyano[bis(2-pyridylmethyl)amine = 2-DPA]ferrate(II) were isolated and their spectroscopic properties compared. The fac-isomer was converted to the corresponding iron(III) complex under acidic conditions. Oxidation of the ferrate(II) complexes with ammonium peroxodisulfate yielded the mer-isomer of the dehydrogenated ferrate(II) compound, but only the metal-oxidized iron(III) complex for the fac-isomer was produced under neutral or basic conditions. Electrochemical measurements confirmed this difference in the oxidation behavior, in which the nature of the coordination governs the ease of oxidative dehydrogenation.

Journal Article↗

Variable strategy toward carbasugars and relatives. 4. Viable access to (4a-carbapentofuranosyl)amines, (5a-carbahexopyranosyl)amines, and amino acids thereof.

A chiral, divergent synthesis of two carbafuranosylamines, 1 and 2, two carbapyranosylamines, 3 and 4, two carbafuranosylamino acids, 5 and 6, and two carbapyranosylamino acids, 7 and 8, has been achieved. Highlights of the procedure include the following: a diastereoselective crossed vinylogous Mukaiyama aldol coupling between N-(tert-butoxycarbonyl)-2-[(tert-butyldimethylsilyl)oxy]pyrrole (TBSOP, 9) and 2,3-O-isopropylidene-D-glyceraldehyde (10) for the assembly of the target compound carbon backbone; a high-yielding silylative cycloaldolization that gives the cyclopentanoid and cyclohexanoid motifs; and a reductive or hydrolytic breakage of the lactam C(O)-N link to liberate the carbasugar and install the desired pseudo-anomeric amine and the hydroxymethyl or carboxyl functionalities. The sequences leading to trans-configured carbafuranosyl compounds 1 and 5 and carbapyranosyl compounds 3 and 7 were 12- and 13-step processes, with overall yields of 34%, 35%, 17%, and 16%. Cis-configured isomers 2, 4, 6, and 8 were obtained only in minor yields.

Journal Article↗

Platelet and plasma amine oxidase inhibition and urinary amine excretion changes during phenelzine treatment.

The treatment of depressed patients with the monoamine oxidase (MAO)-inhibiting antidepressant, phenelzine, was found to be accompanied by an 82 per cent reduction in platelet MAO activity and a 91 per cent reduction in plasma amine oxidase activity. Maximum reductions in enzyme activity occurred after 7 to 14 days of treatment; recovery of enzyme activity posttreatment required an average of 14 days for the platelet MAO and greater than 6 weeks for the plasma enzyme. Marked elevations in urinary tryptamine excretion occurred in conjunction with MAO inhibition during phenelzine treatment, but the magnitidue of urinary tryptamine change in individual patients was not closely correlated with the magnitude of enzyme activity reduction. Changes in platelet serotonin content serotonin content and in urinary catecholamine metabolites also occurred in response to phenelzine treatment.

Blood Platelets↗

Bis[bis(methoxycarbimido)amine-kappa2N,N']bis(perchlorato-kappaO)copper(II) bis[bis(methoxycarbimido)amine-kappa2N,N']bis(methanol-kappaO)copper(II) bis(perchlorate) methanol disolvate.

The title compound, [Cu(ClO4)2(C4H9N3O2)2][Cu(C4H9N3O2)2(CH4O)2](ClO4)2.2CH3OH, comprises two independent Cu(II) species lying on different inversion sites. In the Cu complexes, a distorted octahedral geometry arises (from basic square-planar N4 coordination) from the weak coordination of two perchlorate ions (as Cu-O) in one species and two methanol molecules in the other (also as Cu-O). Interactions between the O atoms of the perchlorate anions or methanol groups and the imide or amine NH groups afford an extensive intermolecular hydrogen-bonding network.

Journal Article↗

[Substances inhibiting amine oxidases. III. Synthesis and amine oxidase inhibition of imidazoquinoline derivatives].

The activity of copper and FAD dependent amine oxidases was tested with some derivatives of 3H-imidazo[4,5-h]quinoline and its isomers 3H-imidazo[4,5-f]quinoline, the chemistry of which is described in the literature (1), and Ki calculated. The methyl derivative of 3H-imidazo[4,5-f]quinoline was found to activate the copper bovine serum enzyme, but inhibits the FAD mitochondrial enzyme.

Animals↗

[Interaction of formaldehyde with nucleic acids and their structural components in the presence of amines. II. Structure of adenine derivatives formed in the reaction with formaldehyde and primary amine].

Two products of modified adenine have been isolated from reaction of adenine with a mixture of formaldehyde and methylamine; their structures have been demonstrated by UV, 1H NMR and mass spectra data. The formal scheme of reaction can be described as simultaneous or sequential cycloaddition of dimethylol derivatives of methylamine to two reaction's positions of the adenine residue. This results in the formation of a new partly or completely hydrogenated six-membered 1,3,5-triazine cycle which has the atoms of adenine nitrogen in its 1,3-positions and nitrogen of methylamine in 5-position. This is used as a model for discussing the peculiarities of DNA-formaldehyde interaction in the presence of amine.

Adenine↗

Activation of N-nitrosobis(2-oxopropyl)amine and N-nitroso(2-hydroxypropyl)-(2-oxopropyl)amine to mutagens for V79 cells by isolated hamster and rat pancreatic acinar cells.

A pancreatic acinar cell-mediated mutagenicity assay was developed as an in vitro model system to study the metabolism of N-nitrosobis(2-oxopropyl)amine (BOP) and N-nitroso(2-hydroxypropyl)(2-oxopropyl)amino (HPOP) into forms mutagenic for Chinese hamster V79 cells. Mutations at the hypoxanthine:guanine phosphoribosyltransferase locus and the Na/K ATPase locus were scored by resistance to 6-thioguanine and ouabain, respectively. The ability of both Syrian golden hamster and Fischer rat pancreatic acinar cells to convert BOP and HPOP to mutagens for V79 cells was investigated in order to examine the basis for species specificity. Acinar cells of both species were capable of activating BOP and HPOP to mutagens for V79 cells in a dose-dependent manner. In the 6-thioguanine resistance assay, rat acinar cells induced higher mutation frequencies than hamster acinar cells with both BOP and HPOP. In the ouabain resistance assay, both cell types induced equivalent levels of mutation with the respective nitrosamines. BOP was a considerably more potent mutagen than HPOP after activation by either cell type. This is consistent with the known in vivo specificity of BOP versus HPOP in the hamster pancreas and suggests that BOP may be activated to mutagenic metabolites by a pathway(s) independent from its enzymatic reduction to HPOP. The comparable abilities of rat and hamster acinar cells to convert BOP or HPOP to mutagenic forms imply that pancreatic metabolic activation alone cannot explain the difference in organotropism of BOP and HPOP in the two species.

Animals↗