Purification and characterization of hepatic porcine gluconolactonase

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Abstract

A divalent metal dependent gluconolactonase has been isolated from porcine liver and purified to apparent homogeneity. Its molecular weight is estimated at 223,000 and that of the subunits is 37,200 as determined by gel electrophoresis. A Km value of 6.2 mM was obtained at 27° in 50 mM tris HCl buffer. Gluconolactonase is specific for gluconolactone, and manganese is preferred over magnesium for maximum activity. The hepatic concentration of gluconolactonase is estimated to be 7.2 μmol of enzyme per kg of porcine liver, and a subcellular fractionation study indicates that this enzyme is located primarily within the cytosol.

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      Several groups of lactonases have been reported (37–39). Among those characterized lactonases, the gluconolactonase of porcine liver and the lactonohydrolase from Fusarium oxysporum require divalent metal ions for activity and are inhibited by metal-chelating reagents (40, 41), whereas others, such as 4- and 5-pyridocolactonase and hydroxyglutaric acid lactonase, are independent of such ions for activity (37, 38). AHL-lactonase appears to belong to the latter.

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