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M Sanchez-Moreno

Publications and source records attributed to M Sanchez-Moreno.

29 records · Page 2Linked to original sources
PubMed1989

Physico-chemical characteristics of superoxide dismutase in Ascaris suum.

1. Three SOD isoenzymes obtained from purified extracts of Ascaris suum were characterized. 2. The physico-chemical characteristics studied were: optimum pH, methods of preservation of enzymatic activity, molecular weight, and the u.v. and visible light absorption spectra. 3. The optimum pH for the Cu, Zn SOD I and II was 10.2 and 10.1 for the Mn SOD. 4. The extracts retained their levels of activity longer at -70 degrees C, and after lyophilization. The Mn SOD was more labile than the Cu, Zn SOD I and II. 5. The molecular weights obtained by filtration through Sephadex G-75 were: 73,000 for Mn SOD; 42,600 for Cu, Zn SOD I; and 39,800 for the Cu, Zn SOD II. 6. Both the u.v. and visible light spectra were similar to other dismutases from other sources.

Animals↗
PubMed1989

Superoxide dismutase in cestodes. Isoenzymatic characterization and studies of inhibition by a series of benzimidazoles and by pyrimidine derivatives of recent synthesis.

The activities of superoxide dismutase (SOD) (E.C.1.15.1.1) in extracts of five cestode parasites (Moniezia expansa, M. benedeni, Avitellina centripunctata. Taenia hydatigena and Dipylidium caninum) were investigated. The polyacrylamide gel electrophoretic patterns revealed that each of the five species had four isoenzyme bands; they could be differentiated principally by their displacements and, less clearly, by their intensities. Determinations were made of the inhibitory activities of four benzimidazoles and six recently synthesised pyrimidine derivatives on the SOD enzymes from the cestodes. The results confirm that the percentage of inhibitions of SOD by the same pyrimidine derivatives are markedly superior to those of the benzimidazoles.

Animals↗
PubMed1988

Superoxide dismutase activity in extracts of specimens of Ascaris suum and several analogous tissues in both sexes.

1. The activities of the enzymes superoxide dismutase (EC.1.15.1.1), and catalase (EC.1.11.1.6) in purified extracts of whole Ascaris suum adult males and females, and also in several analogous tissues of each sex, were studied. 2. No catalase activity was found in any of the extracts. 3. Considerable superoxide dismutase activity was detected in both sexes and the levels of this activity showed sexual differences in the values found in different tissue locations. 4. The sexual organs of both males and females showed the highest SOD activity of all the tissues examined. 5. Polyacrylamide gel electrophoresis pattern analysis confirmed that the female tissues had more SOD enzyme components than the corresponding tissues in the male.

Animals↗
PubMed1988

Superoxide dismutase from Ascaris suum.

Three superoxide dismutases (SOD) (EC 1.15.1.1) were detected in homogenates of Ascaris suum. Each of the three forms of SOD was purified by a sequence of multiple differential centrifugations, ammonium sulphate precipitation, ion-exchange chromatography and G-75 Sephadex column chromatography. The three forms of SOD were present in different cellular locations; one in the cytoplasmic fraction, sensitive to cyanide and hydrogen peroxide, and two in the mitochondrial fraction, one of which was cyanide sensitive. The SOD forms presented clear differences in their electrophoretic patterns. The sexual organs of females showed the highest SOD activities of all the tissues examined. The finding of such high levels of superoxide dismutase in A. suum reflects the importance of this enzyme in the metabolism of this helminth parasite.

Animals↗
PubMed1988

Fasciola hepatica and Dicrocoelium dendriticum: isoenzyme patterns of malate dehydrogenase and malic enzyme.

The MDH isoenzymes and ME isoenzymes (EC.1.1.1.39) in two helminth parasites, F. hepatica and D. dendriticum, obtained from two host species (Capra hircus and Ovis aries), were studied by electrophoresis on polyacrylamide gels. F. hepatica MDH showed three isoenzymatic bands; D. dendriticum MDH, only two. No difference was noted between the enzyme profiles, or the densitometric scans in samples from specimens from different host species. F. hepatica ME presented three bands, that of D. dendriticum, only two. Only in F. hepatica were differences observed between the enzyme profiles of specimens obtained from the different host species.

Animals↗
PubMed1987

Inhibition of malate dehydrogenase enzymes by benzimidazole anthelmintics.

Determinations were made of the inhibitory activities of four benzimidazole anthelmintics (Albendazole, Parbendazole, Mebendazole and Thiabendazole) on purified extracts of cytoplasmic and mitochondrial malate dehydrogenase obtained from Ascaris suum, Fasciola hepatica and Moniezia expansa. The highest percentage inhibitions were exhibited by Mebendazole. The results confirm that cytoplasmic MDH and mitochondrial MDH regulator enzymes of glycogen synthesis are the sites of mebendazole inhibitory activity, but the activity sites of the other anthelmintics in the study remain unclear.

Albendazole↗
PubMed1987

Superoxide dismutase activity in nematodes.

The activities of the enzymes superoxide dismutase (E.C.:1.15.1.1) and catalase (E.C.:1.11.1.6) were studied in purified extracts of four nematodes: Ascaris suum, Toxascaris leonina, Toxocara canis and T. cati adult males and females. No catalase activity was found in any of the extracts. The results reveal that the SOD activities of the four parasites presented species differences and also sexual differences within each species. Polyacrylamide gel electrophoresis pattern analysis confirmed that the mobilities, widths and band intensities varied according to the species and sex of the parasite from which the enzyme was obtained.

Animals↗
PubMed1987

Malate dehydrogenase in helminth parasites. Inhibition by benzimidazoles and pyrimidine derivatives.

A study was performed of the activities of both cytoplasmic and mitochondrial, malate dehydrogenase (MDH) (E.C.1.1.1.37) in purified extracts of whole specimens of male and female nematodes of four species: T. canis, T. cati, T. leonina and A. suum (and tissues), two trematodes: F. hepatica and D. dendriticum, and four cestodes: M. expansa, M. benedeni, D. caninum and T. hydatigena. The results show that there exist species and sexual differences in the enzyme activities of both enzymes. The relative importance of this energy pathways of these helminth species is discussed. Determinations were made of the in vitro inhibitory activities of four benzimidazoles and six synthesised pyrimidine derivatives on MDH (soluble and mitochondrial) from helminth parasites. Several pyrimidine derivatives (6-amino-5-methyl-5-nitro-uracil, 4-amino-1-methyl-2-methylthio-5-nitro-6-oxo-1,2,3,4-tetrahydropyrimid ine and 4-amino-2-methylthio-5-nitro-6-oxo-1,2,3,4-tetrahidropyrimidine) produced double percent in vitro inhibitions of those shown by the benzimidazoles.

Animals↗
PubMed1987

Superoxide dismutase in trematodes. Isoenzymatic characterization and studies of inhibition by a series of benzimidazoles and by pyrimidines of recent syntheses.

A comparative study was carried out of superoxide dismutase (E.C.1.15.1.1) (SOD) and catalase activities in purified extracts of two trematodes: Fasciola hepatica and Dicrocoelium dendriticum. The superoxide dismutase activity was very similar to that measured in other eukaryotic cells. As no catalase activity was detected, the possibility that SOD in these trematodes might have the particular importance of removing superoxide radicals is discussed. The SOD isoenzymes of each species were analysed by polyacrylamide gel electrophoresis and the patterns revealed a quantitative difference in the number of isoenzyme bands: F. hepatica showed three, and D. dendriticum only two. Determinations were made of the in vitro inhibitory activities of four benzimidazoles and six synthesised pyrimidine derivatives on SOD from trematodes. The present results confirm that the percentage inhibitions of the pyrimidine derivatives are markedly superior to those produced by the benzimidazoles.

Animals↗