Molecular heterogeneity of plasma superoxide dismutase.

A method was worked out that helped us to isolate superoxide dismutase (SOD) from human blood plasma. The change of enzyme's activity was shown depending on the period of SOD storage. Changes in activity were observed in storing protein after gel filtration. The activity of purified enzyme was half as much after 24 h storage and remained constant for a long period of time (5 mo). The change of SOD activity was found to be connected with a modification of its structure. The storage of enzyme's solution during 3 1/2 mo is accompanied by the lowering of protein molecular mass from 53,000 Da to 34,000 Da. The inhibitors of proteinases--phenyl-methylsulfonyl fluoride (PMSF) and alpha 2-macroglobulin--showed no protective effects on purified SOD. That's why it was possible to say that the lowering of protein molecular mass didn't connect with a specific proteolysis. An oxidative modification of SOD structure is under discussion now. The modification is most probably caused by oxidative destruction of aminoacid residues that are located outside the protein active centre.