Major hemolymph protein (MHP) was purified from larval hemolymph of Galleria mellonella by KBr density gradient ultracentrifugation, ion exchange chromatography (DEAE-Trisacryl M), YM-50 ultrafiltration and gel permeation chromatography (Sephadex G-100). MHP is composed of two subunit (MHP-l and MHP-2). The molecular weights of each subunit were determined (MHP-l = 86kDa and MHP-2 = 84kDa). MHP is present in both hemolymph and fat body during developmental stages, indicating this protein is carrying out some functions different from other major protein such as storage protein and lipophorin.