Cu-Zn-superoxide dismutase activity in Moniezia expansa: inhibition by pyrimidine derivatives.
Copper-zinc, cyanide-sensitive superoxide dismutase (Cu-Zn-SOD) was detected in homogenates of Moniezia expansa. The enzyme was purified by a sequence of multiple differential centrifugations, ammonium sulphate precipitation, ion-exchange and G-75 Sephadex column chromatography. The final enzyme preparation had a specific activity of 623.00 +/- 9.97U per mg protein and, after isolation, a single-staining band on acrylamide-SDS gels was detected which coincided with enzyme activity. The inhibitory activities of several benzimidazoles and several novel pyrimidine derivatives were determined on purified extracts of the M. expansa Cu-Zn-SOD. The results indicated that the percentage inhibition of Cu-Zn-SOD by some pyrimidine derivatives (6-amino-1, 3-dimethyl-5-nitroso-uracil, 6-amino-5-methyl-5-nitroso-uracil and 5-amino-uracil) was markedly higher than inhibition with the benzimidazoles.
Sanchez-Moreno
M
M
Ortega
J E
JE
Sanchez-Navas
A
A
Salas-Peregrin
J M
JM
Monteoliva
M
M
D000818:Animals; D002589:Cestoda / Q000187:drug effects / Q000201:enzymology*; D008989:Monieziasis / Q000469:parasitology; D011743:Pyrimidines / Q000494:pharmacology*; D013482:Superoxide Dismutase / Q000037:antagonists & inhibitors*
D011743:Pyrimidines; D013482:Superoxide Dismutase