Inhibition of human NTPDase 2 by modification of an intramembrane cysteine by p-chloro-mercuriphenylsulfonate and oxidative cross-linking of the transmembrane domains

The studies about the human NTPDase 2 activity, which is inactivated by membrane perturbation that disrupts interactions of the transmembrane domains and inhibited by p-chloro-mercuriphenylsulfonate (pCMPS), a sulfhydryl reagent are reported. The loss of the ATPase activity of human NTPDase 2 in the presence of pCMPS possibly results from the disturbance of both transmembrane domain interaction and its active site and is attenuated when the enzyme is cross-linked by glutaraldehyde.