Purification and Properties of Phospholipase A1Produced byCorticium centrifugum

Publisher Website
Google Scholar
Abstract
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, 1-propanol and Triton X–100 stimulated phospholipase A1 activity, these substances showed an inhibitory effect against lysophospholipase 1 activity. Phospholipase A1 activity was almost completely inhibited by Fe2+, Fe3+ and Al3+, but the inhibition was lessened by the presence of Triton X–100. Lysophospholipase 1 activity was inhibited by Hg2+, Fe3+ and Al3+. The mode of inhibition by Fe3+ against lysophospholipase 1 activity was apparently an uncompetitive type. Phospholipase A1 hydrolyzed various phospholipids, but not triolein.

This publication has 4 references indexed in Scilit: