Abstract
Rhizopus C-lipase displayed appreciable triglyceride-hydrolyzing activity upon isolated human plasma lipoproteins after treatment with a phospholipid. Treatment of the lipase with phosphatidylcholine or cardiolipin was most effective in enhancing the activity on these substrates. The treated enzyme acted equally well on any of three lipoproteins, chylomicron, very low density lipoprotein (pre-β) and low density lipoprotein (β).
