Absence of 5'-nucleotidase in porcine polymorphonuclear leucocyte membranes.


A fraction enriched in plasma membranes from porcine polymorphonuclear leucocytes, isolated by sucrose density centrifugation was shown to possess considerable AMP hydrolysing activity (150 nmol/min per mg protein). However all of this activity could be inhibited using excess p-nitrophenyl phosphate in the incubation medium. Furthermore the hydrolysis of AMP by the membrane was unaffected by the 5'-nucleotidase inhibitor alpha, beta-methyleneadenosine diphosphate and by the lectin concanavalin A, another potent inhibitor of 5'-nucleotidase. An antibody against mouse liver 5'-nucleotidase also did not inhibit the activity. These results suggest that the hydrolysis of AMP by porcine polymorph membranes is not accomplished by a specific 5'-nucleotidase and the necessity for distinguishing between true 5'-nucleotidase and non-specific phosphatase activity is discussed.

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@article{Castle1982AbsenceO5, title={Absence of 5'-nucleotidase in porcine polymorphonuclear leucocyte membranes.}, author={Amanda Castle and Rakesh Chibber}, journal={Biochimica et biophysica acta}, year={1982}, volume={688 2}, pages={637-44} }