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Eclosion hormone of the silkworm Bombyx mori Expression in Escherichia coli and location of disulfide bonds
Author(s) -
Kono Takaharu,
Nagasawa Hiromichi,
Kataoka Hiroshi,
Isogai Akira,
Fugo Hajime,
Suzuki Akinori
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81413-i
Subject(s) - bombyx mori , escherichia coli , disulfide bond , biochemistry , thermolysin , bombycidae , chemistry , bombyx , cysteine , gene , biology , enzyme , trypsin
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 NH 2 ‐terminal are dispensable but 4 residues at the COOH‐terminal play an important role in EH activity.