Haemoglobin adducts of aromatic amines: diamines and polyaromatic amines

Aromatic amines and nitroarenes are important antioxidants and intermediates in the synthesis of dyes, pesticides and plastics. In the present paper we introduce methods for the synthesis of deuterated standards: 3-[²H₈]aminofluoranthene, 3,3′-dimethyl-[²H₄]benzidine, [²H₄]benzidine, N′-acetyl-[²H₄]benzidine, 2,4-[²H₆]toluenediamine, 2,6-[²H₆]toluenediamine. These standards have been used for the quantification of haemoglobin adducts of diamines and polyaromatic amines. Haemoglobin was hydrolysed in 0.1 M sodium hydroxide and the hydrolysate extracted with dichloromethane. The extracts were derivatised with heptafluorobutyric anhydride and analysed by GC–MS with negative chemical ionisation. In one run up to 15 aromatic amines can be determined: 6-aminochrysene, 3-aminofluoranthene, 2-aminofluorene, 1-aminopyrene, benzidine, 3,3′-dichlorobenzidine, 3,3′-dimethoxybenzidine, 3,3′-dimethylbenzidine, 3,3′-methylenedianiline, 4,4′-methylenedianiline, N′-acetyl-benzidine, N′-acetyl-4,4′-methylenedianiline, 4,4′-methylene bis(2-chloroaniline), 2,4-toluenediamine and 2,6-toluenediamine.     

Electromigration methods for amino acids, biogenic amines and aromatic amines

Methods of electromigration in laboratory apparatus of small-bore size have recently undergone development at a remarkably rapid pace, leading to a variety of new analytical techniques. One such technique is called “capillary electrophoresis” (CE), which is further classified on the basis of electromigration mode, viz., “capillary zone electrophoresis” (CZE), which, in turn, has several variations. This review aims to give a short overview of the various electromigration methods for amino compounds by using CE. Firstly, this review briefly summarizes the detection methods employed for detection of monoamines and polyamines by CE for both native and derivative forms. Next, current CE methods are described, and their applications to detection of amino acids, biogenic amines, aromatic amines, including heteroaromatic amines and their enantiomers, are introduced from representative papers. Finally, new methods for single-cell analysis and microchip CE techniques are focused on.     

Utilization of amines by yeasts

461 Strains of the yeast collection of the Centraalbureau voor Schimmelcultures (CBS) were screened for their ability to utilize 9 different amines as a sole carbon and energy source and/or as nitrogen source. A miniaturized technique with microtiter plates was used. None of the primary and methylated amines tested (i.e. methylamine, dimethylamine, trimethylamine, tetramethylammonium chloride, choline, ethylamine, propylamine, butylamine and benzylamine) were utilized as a carbon and energy source, although the majority of yeasts (86%) were able to utilize one or more of these compounds as a nitrogen source. The ability to utilize ethylamine and higher homologues occurred more frequently than the ability to utilize methylated amines. In almost all genera the utilization of primary and methylated amines was found, with utilizing and non-utilizing species occurring within a genus. The occurrence of specific assimilation patterns of amine utilization among yeasts and the inability of these organisms to utilize amines as a carbon and energy source is discussed.     

Microsomal-catalyzed hydroperoxide-dependent C-oxidation of amines

Organic hydroperoxides are capable of supporting the C-oxidation of several different amines in the presence of hepatic microsomes. Evidence is presented that indicates that microsomal cytochrome P-450 acts as the catalyst. Removal of the NADPH-cytochrome $\text{c}$ oxidoreductase or essential phospholipid from microsomes does not significantly affect the peroxidase activity. Of the amine substrates C-oxidized by organic hydroperoxides in the presence of microsomes, only aminopyrine and dimethylaniline are rapidly oxidized by hydroperoxides in the presence of catalase. The catalase-mediated reaction can also be distinguished from the microsomal-catalyzed reaction by the use of differential inhibitors.     

Polymers of biogenic amines.

Biogenic amines, with a primary amino group, were reacted with glutaraldehyde to form insoluble precipitates. These precipitates had distinctive ultrastructural features upon further reaction with osmic acid. When tested in vitro, they had biological activity and showed evidence that part of this biological activity was due to the large polymer of glutaraldehyde and amine. Experiments with isotope-labelled amines in the production of these precipitates showed that the precipitated polymers were not completely stable and that free amine was liberated from them. Since they were not stable, , they could not be used for the morphological localization of the amines as had been intended, but they may have some use as depot drugs or in the immunization of animals against these amines.     

Oxidation of amines by flavoproteins

Many flavoproteins catalyze the oxidation of primary and secondary amines, with the transfer of a hydride equivalent from a carbon-nitrogen bond to the flavin cofactor. Most of these amine oxidases can be classified into two structural families, the D-amino acid oxidase/sarcosine oxidase family and the monoamine oxidase family. This review discusses the present understanding of the mechanisms of amine and amino acid oxidation by flavoproteins, focusing on these two structural families.     

Biogenic amines in coelenterates

1. This mini review highlights the most important findings during three decades of research on biogenic amines in coelenterates.2. Histochemical, analytic chemical and physiological evidences clearly indicate that dopamine is used as an intercellular messenger in hydrozoans.3. The colonian anthozoan Renilla, has β-adrenergic mechanisms in monitoring bioluminescence and serotoninergic mechanisms in rhythmic contractions.     

Assay of biogenic amines by bioluminescence

A bioluminescent procedure to measure noradrenaline and serotonin has been realized. The amines are oxidized by the monoamine oxidase of pig brain mitochondria. The NH3 generated in this reaction is directly measured by enzymatic reaction. The coenzyme of this last reaction is the NADH,H+ which is measured with a bioluminescent system: the FMN-oxidoreductase-luciferase. The extension to other amines is possible, it depends only of the specificity of the monoamine oxidase.     

Conjugation of chondroitin sulfates with amines

Conjugation of chondroitin sulfates with pharmacologically important amines in a water medium in the presence of 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide was studied. Conjugates with amide and isoureidocarbonyl groups were synthesized. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2008, vol. 34, no. 5; see also http://www.maik.ru