ABSTRACT
The effect of CulZn superoxide dismutases from yeast cells (SODy) and commercial SOD from bovine erythrocytes (SODb) on zymosan-induced inflammation in mice and on complement activity in normal human serum (NHS) was studied. Zymosan-induced oedema formation was moderately suppressed by SODb. The alternative pathway (AP) activity in mouse serum was strongly inhibited after i.p. treatment with SODy. Comparison between the two enzymes showed different mode of action on the classical pathway (CP) as compared to the AP of complement activation. The inhibitory effect caused by SODy was more pronounced and strongly time- and temperature-dependent. SODy affected several activation steps in the complement cascade, while the inhibition caused by SODb was mainly directed to C1 of the complement activity. The powerful action of SODy on AP activity may be attributed to the oligosaccharide moiety in the enzyme molecule from yeast origin.
