Abstract
Summary
1. A twenty-fold purification of staphylococcal penicillinase, based upon specific activity, has been achieved. The enzyme, from a penicillin resistant strain of S. aureus, was freed from the cells by grinding with glass beads and purified by ammonium sulfate fractionation and precipitation with ethanol. Brown crystals of indefinite shape have been obtained by the procedure outlined. 2. The purified, crystalline, penicillin-ase was subjected to electrophoresis at pH 5.0 and 8.6. Only one band was observed. At both pH's this band migrated the same distance from the origin as did a partially purified preparation of B. cereus penicillinase. 3. Precipitin tests showed an immuno-logical cross reaction between the enzymes. Inhibition studies however indicated possible differences. Staphylococcal penicillinase activity was inhibited by both homologous and heterologous antiserum. B. cereus penicillin-ase was neutralized to lesser degree by the heterologous antiserum.
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