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Purification of Major Hemolymph Protein of Great Wax Moth, Galleria mellonella
Author(s) -
JOE JunHo,
YUN Hwa Kyung
Publication year - 2004
Publication title -
entomological research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.421
H-Index - 20
eISSN - 1748-5967
pISSN - 1738-2297
DOI - 10.1111/j.1748-5967.2004.tb00110.x
Subject(s) - galleria mellonella , hemolymph , biology , ultrafiltration (renal) , sephadex , gel permeation chromatography , molecular mass , wax , protein subunit , chromatography , ultracentrifuge , biochemistry , chemistry , enzyme , organic chemistry , virulence , gene , polymer
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‐1 and MHP‐2). The molecular weights of each subunit were determined (MHP‐1 = 86 kDa and MHP‐2 = 84 kDa). 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.