Purification of sarcotoxin III, a new antibacterial protein of Sarcophaga peregrina.
A glycine-rich antibacterial protein with a molecular mass of 7,000 termed sarcotoxin III, was purified to homogeneity from the hemolymph of third instar larvae of Sarcophaga peregrina. When the hemolymph was fractionated, this protein was recovered in the same fraction as sarcotoxin I, a group of potent antibacterial proteins that have been purified. But, it was clearly different from sarcotoxin I in amino acid composition and molecular mass. Sarcotoxin III was shown to be induced in the hemolymph in response to injury of the larval body wall.
Baba
K
K
Faculty of Pharmaceutical Sciences, University of Tokyo.
Okada
M
M
Kawano
T
T
Komano
H
H
Natori
S
S
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000900:Anti-Bacterial Agents / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D004175:Diptera; D004926:Escherichia coli / Q000187:drug effects; D006458:Hemolymph; D007301:Insect Hormones / Q000302:isolation & purification* / Q000494:pharmacology; D019476:Insect Proteins; D007814:Larva; D008970:Molecular Weight
D000596:Amino Acids; D000900:Anti-Bacterial Agents; D007301:Insect Hormones; D019476:Insect Proteins; C054070:sarcotoxin III protein, Sarcophaga peregrina