PURIFICATION AND PROPERTIES OF PHOSPHOLIPASE-A1 PRODUCED BY CORTICIUM-CENTRIFUGUM

Phospholipase A1, purified from the culture filtrate of Corticium centrifugum. was found to possess lysophospholipase 1 activity. The isoelectric point was pH 3.3, and the molecular weight was about 26,800. Both enzyme activities had their pH optimum between 4.0 and 4.5 and their pH stability between 6.0 and 8.0, and were heat-unstable. Both were inhibited by p-diazobenzenesulfonic acid and N-bromosuccinimide. Although ether, I-propanol and Triton X-100 stimulated phospholipase A1activity, these substances showed an inhibitory effect against Iysophospholipase I activity. Phospholipase A1activity was almost completely inhibited by Fe2+, Fe3+and Al3+, but the inhibition was lessened by the presence of Triton X-10a. Lysophospholipase 1 activity was inhibited by Hg2+, Fe3+and Al3+. The mode of inhibition by Fe3+against Iysophospholipase I activity was apparently an uncompetitive type. Phospholipase A1hydrolyzed various phospholipids, but not triolein. © 1979 Taylor & Francis Group, LLC.