Eclosion hormone of the silkworm Bombyx mori. Expression in Escherichia coli and location of disulfide bonds.
A gene encoding eclosion hormone (EH) from the silkworm, Bombyx mori was chemically synthesized, inserted into a secretion vector and expressed in Escherichia coli, leading to the production of biologically active EH. Sequence analysis of cystine-containing peptides in a thermolysin digest of this EH established the locations of 3 disulfide bonds in the molecule. Evidence was also obtained that the 6 residues at the NH2-terminal are dispensable but 4 residues at the COOH-terminal play an important role in EH activity.
Department of Agricultural Chemistry, Faculty of Agriculture, University of Tokyo, Japan.
T
T
Kono
H
H
Nagasawa
H
H
Kataoka
A
A
Isogai
H
H
Fugo
A
A
Suzuki
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D012831:Bombyx; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides / Q000032:analysis; D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression; D007301:Insect Hormones / Q000235:genetics / Q000302:isolation & purification; D008969:Molecular Sequence Data; D015394:Molecular Structure; D013820:Thermolysin; D014162:Transfection
D004220:Disulfides; D007301:Insect Hormones; C042645:eclosion hormone; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D013820:Thermolysin