Efficient production of N-terminally truncated biologically active human interleukin-6 by Bacillus brevis

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 bre...

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Published inBioscience, biotechnology, and biochemistry Vol. 64; no. 3; pp. 665 - 669
Main Authors Shiga, Y. (Tokyo Univ. of Pharmacy and Life Science, Hachioji (Japan)), Maki, M, Ohta, T, Tokishita, S, Okamoto, A, Tsukagoshi, N, Udaka, S, Konishi, A, Kodama, Y, Ejima, D, Matsui, H, Yamagata, H
Format Journal Article
LanguageEnglish
Published Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.03.2000
Japan Society for Bioscience Biotechnology and Agrochemistry
Oxford University Press
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Summary: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
Bibliography:F60
2000006077
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ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.64.665