The activity of several antioxidant and detoxifying enzymes, superoxide dismutase SOD, GSH peroxidase GSHPx, GSSG reductase GSR and GSH S transferase GST, the contents of thiobarbituric acid reactive substances TBARS, and the SOD and GST isoenzyme patterns were studied in the livers of chubs Leuciscus cephalus from reference river areas and polluted urban sites. Livers of polluted fish contained higher concentrations of transition metals, especially copper and iron. Total GSHPx activity was 1.8 fold higher in the polluted fish than in reference animals, while the SOD and GSR activities and the TBARS content were not significantly changed. Three new SOD isoforms pI 4.45, 5.1, 5.2 and a higher intensity of the band pI 4.2 were observed after isoelectrofocusing of polluted fish extracts. Total GST activity was higher in fish from polluted areas. The GST isoenzyme pattern was studied using subunit specific substrates DCNB, EPNP, EA, NPB, NBC and by Western blot using antibodies specific to rat GST subunits 1, 8 Alpha class, 3 Mu class and 7 Pi class. Reference and polluted fish lacked cross reactivity towards Alpha class GSTs. Reference fish displayed weaker cross reactivity towards CST 7 and 2.3 fold lower activity with EA, while higher cross reaction with GST 3 was observed in polluted fish.
Isoenzyme patterns of lactate dehydrogenase (EC 1.1.1.27) in avian sera are described and compared with those of carp and some mammals. The predominant portion of lactate dehydrogenase in avian sera was concentrated in the muscular form of the enzyme (lactate dehydrogenase 5). Most mammalian sera (with the exception of rat serum) showed a different pattern, in which the main portion of lactate dehydrogenase activity migrated in the first three anodic fractions. Fish serum lactate dehydrogenase isoenzymes were distributed similarily to those of mammals. The electrophoretic mobility of bird lactate dehydrogenase isoenzymes in a pH gradient of 3 to 9 was different from that of carp, cattle and rabbit. Bird lactate dehydrogenase isoenzymes were localized in the pH region of 5.8 to 8.1. In contrast, the mammalian isoenzymes were more acidic, with pi values in the range of 4.5 to 7.3. Lactate dehydrogenase isoenzymes of carp migrated in a narrow pH range of 5.2 to 6.5.
We developed a new HPLC method for the determination of p-aminobenzoic acid (PABA) and its metabolites (p-aminohippuric acid, N-acetyl-p-aminohippuric acid, N-acetyl-p-aminobenzoic acid) in urine. As the internal standard m-hydroxybenzoic acid was used. In the isocratic elution the mobile phase consisted of methanol and 0.02 M ammonium acetate (20:80 v/v, pH 4.0). The separation was carried out on the C18, reversed-phase column, particle size 5 microns. The separated components were detected at 280 nm. The method can be used in the assessment of the response of pancrease (secretion of digestive enzymes) to soya feeding as well as in the diagnosis of the exocrine pancreatic diseases of animals.
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