Eclosion hormone of the silkworm Bombyx mori Expression in Escherichia coli and location of disulfide bonds

FEBS Letters

Kataoka, Hiroshi¹  Fugo, Hajime¹  Nagasawa, Hiromichi¹  Kono, Takaharu¹  Isogai, Akira¹  Suzuki, Akinori¹ 

[1] Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo, Bunkyo-ku, Tokyo 113 Japan

关键词: Eclosion hormone;    Insect peptide hormone;    Synthetic gene;    Disulfidebond;    Bombyx mori;    EH;    eclosion hormone;    RP-HPLC;    reverse-phase high-performance liquid chromatography;    ELISA;    enzyme-linked immunosorbent assay;   

DOI  :  10.1016/0014-5793(90)81413-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown