Purification and characterization of epidermis-origin hemolymph protein in Galleria mellonella.
Epidermis-origin hemolymph protein (EOHP) was identified and purified from the last instar larval hemolymph of Galleria mellonella by anion exchange chromatography, chromatofocusing chromatography, and Sephadex G-100. The EOHP has a native molecular mass of 47 kDa and is composed of one subunit. The isoelectric point of the EOHP was determined to be 5.3. The amino acid composition of the EOHP was rich in aspartic acid, glutamic acid and lysine, but poor in tyrosine, methionine, and tryptophan. EOHP is present in hemolymph over the period from the 4th instar larvae to the adult stage examined. Concentration of EOHP is high during the larval stage but gradually decreased during the developmental stage from pupal to adult stage. EOHP is present in the cuticle, fat bodies and trachea but not in hemocytes, fore gut, mid gut and hind gut.
Lee
Y H
YH
Department of Biology, Korea University, Seoul, South Korea.
Lee
H Y
HY
Kim
H R
HR
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001412:Bacillus subtilis / Q000187:drug effects; D015180:Electrophoresis, Gel, Two-Dimensional; D004817:Epidermis / Q000737:chemistry; D004926:Escherichia coli / Q000187:drug effects; D006458:Hemolymph / Q000737:chemistry; D019476:Insect Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D007526:Isoelectric Point; D007814:Larva / Q000737:chemistry; D008970:Molecular Weight; D009036:Moths / Q000737:chemistry*
D000596:Amino Acids; D019476:Insect Proteins