[NADPH-containing, superoxide-producing lipoprotein fraction from blood serum. Isolation, purification, brief characteristics and mechanism of action].

A procedure for isolation and purification of the lipoprotein fraction from blood serum (human, rabbit, bovine, rat) has been developed which includes ion-exchange chromatography of the dialyzed serum on DEAE and CM cellulose and DEAE. Sephadex as well as gel filtration on Sephadex G-150 and biogel P-150. This fraction was purified until denaturation and loss of solubility. The optical purification index of this fraction (A280/A430) is 8.5. The fraction has an optical absorption spectrum with a maximum at 280 nm and a weakly expressed shoulder at 430 nm, its fluorescence spectrum has an excitation maximum at 370 nm and emission maximum at 430 nm characteristic of NADPH. The protein fraction presumably contains NADPH and about 50% of phospholipids. It is assumed that the mechanism of O2 production involves Fe3+ reduction to Fe2+ by NADPH and the electron transfer from Fe2+ to atmospheric oxygen. Suprol provides a simple and readily accessible source of superoxide radicals for the study of their effects on various biosystems.