Abstract
Freshwater mussel Lamellidens marginalis showed a Ca 2+-stimulated ATPase activity in the microsomal fraction of gill. Mg 2+ was also found to be an activating cation for this ATPase enzyme. Ca 2+ ATPase showed maximal activity at 40 °C and between pH 7.5–8.0. Substrate specificity of Ca 2+ ATPase was highest with ATP, followed by GTP and other trinucleotides such as UTP, CTP and ADP also showed some amount of hydrolysis. Ca 2+ ATPase showed slight inhibition with ruthenium red and sodium vanadate and is insensitive to sodium azide, ouabain, oligomycin B and phenylalanine. Heavy metals like Hg 2+, Cu 2+ and Zn 2+ showed 50% inhibition of Ca 2+ ATPase activity at concentrations of 0.25 mM, 0.5 mM and 1 mM, respectively whereas Cd 2+ and Ni 2+ showed 39% and 28% inhibition of enzyme activity at 1 mM concentrations.
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