Kono T, Nagasawa H, Kataoka H, Isogai A, Fugo H, Suzuki A
Department of Agricultural Chemistry, Faculty of Agriculture, University of Tokyo, Japan.
FEBS Lett. 1990 Apr 24;263(2):358-60. doi: 10.1016/0014-5793(90)81413-i.
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.
