Efficient Production ofN-terminally Truncated Biologically Active Human Interleukin-6 byBacillus brevis | Zendy

Yasuhiro Shiga | Zendy; Makiko MAKI | Zendy; Toshihiro Ohta | Zendy; Shinichi Tokishita | Zendy; Akou OKAMOTO | Zendy; Norihiro Tsukagoshi | Zendy; Shigezo Udaka | Zendy; Atsushi KONISHI | Zendy; Yuko Kodama | Zendy; Daisuke Ejima | Zendy; Hiroshi Matsui | Zendy; Hideo Yamagata | Zendy

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Efficient Production ofN-terminally Truncated Biologically Active Human Interleukin-6 byBacillus brevis

Author(s) -

Yasuhiro Shiga,

Makiko MAKI,

Toshihiro Ohta,

Shinichi Tokishita,

Akou OKAMOTO,

Norihiro Tsukagoshi,

Shigezo Udaka,

Atsushi KONISHI,

Yuko Kodama,

Daisuke Ejima,

Hiroshi Matsui,

Hideo Yamagata

Publication year - 2000

Publication title -

bioscience biotechnology and biochemistry

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.64.665

Subject(s) - signal peptide , biological activity , bacillus (shape) , secretion , biology , biochemistry , microbiology and biotechnology , chemistry , peptide sequence , in vitro , gene

cDNAs encoding human interleukin 6 (hIL-6) and its variants lacking the N-terminal Pro and Pro-Val-Pro-Pro, respectively, were expressed in Bacillus brevis by using the signal peptide fusion approach. The presence of Pro at the N-terminus of the mature protein hindered the action of the Bacillus brevis signal peptidase. hIL-6 lacking the N-terminal Pro-Val-Pro-Pro was most efficiently secreted in a biologically active form and accumulated in the culture medium to a level of 200 mg per liter, which is the highest level reported for the bacterial secretion of hIL-6.

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