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Purification of a human alternative complement pathway inhibitor from hemolymph of larval fall armyworm (Spodoptera
Biochemical and Biophysical Research Communications
|August 16, 1984
Abstract:
Larval Spodoptera frugiperda hemolymph contains a specific inhibitor of the alternative pathway of human complement. This inhibitor was purified from larval hemolymph (HL) by 50% (NH4)2SO4 precipitation, DEAE-Sephacel chromatography and sequential gel-filtration on Bio-Gel 1.5m, 0.5m and Sephacryl S-200. Purified HL protein (Mr = 110,000) was composed of two Mr 55,000 polypeptide chains. Addition of purified HL protein to human complement resulted in a dose-dependent inhibition of RaRBC lysis and clumping of cells. The protein inhibitor provides a new tool for investigating the regulation of human alternative complement pathway.