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J. Biol. Chem., Vol. 255, Issue 3, 1227-1233, 02, 1980
D LeBel, GG Poirier, S Phaneuf, P St.-Jean, JF Laliberte and AR Beaudoin
An ATP diphosphohydrolase (EC 3.6.1.5) from the pancreas of the pig has
been characterized and purified. The enzyme which has an optimum pH between
8 and 9 is specific for diphospho- and triphosphonucleosides. The Km values
for ADP and ATP are 7.4 and 7.3 x 10(-4) M, respectively, and the purified
enzyme has specific activities of 13 and 15.2 mumol of Pi/min/m of protein,
respectively. It requires calcium or magnesium ions and it is insensitive
to ATPase inhibitors, namely oligomycin, ouabain, and ruthenium red, and to
levamisole, an inhibitor of alkaline phosphatase. Denaturation experiments,
by heat and trypsin treatments, indicated that only one enzyme is involved.
This is confirmed by the solubilization and purification process and by
polyacrylamide gel electrophoresis. A 270-fold purification was obtained by
centrifugation and successive column chromatography on Sepharose 4B and
Affi-Gel blue. It is a glycoprotein with a molecular weight of 65,000 as
estimated by polyacrylamide gel electrophoresis.
Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas
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