In vitro inhibition of Ca+2 ATPase by methylparathion in prawn: a kinetic approach.
After in vitro addition of IC50 concentration of methylparathion on Ca+2 ATPase in nervous and hepato-pancreatic tissues of prawn were studied. The inhibitory pattern of Ca+2 ATPase elucidate the interaction of methylparathion with ATPase system. The significant decrease in maximal velocity (Vmax) without appreciable change in apparent Michaelis-Menten constant (Km) suggests that the impact of methylparathion on Ca+2 ATPase is independent of substrate and is of a classical non-competitive type.
Reddy
M S
MS
Department of Marine Zoology, Sri Venkateswara University Post-Graduate Centre (A.P), India.
Rao
K V
KV
D000818:Animals; D001693:Biological Transport, Active; D002118:Calcium / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors*; D033364:Decapoda / Q000187:drug effects* / Q000201:enzymology; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008743:Methyl Parathion / Q000494:pharmacology*; D008928:Mitochondria; D009417:Nerve Tissue / Q000201:enzymology; D009498:Neurotoxins; D010179:Pancreas / Q000201:enzymology
D009498:Neurotoxins; D008743:Methyl Parathion; D000252:Calcium-Transporting ATPases; D002118:Calcium