Cell Structure and Function | |
The Substitution of Cysteine 17 of Recombinant HumanG-CSF with Alanine Greatly Enhanced its Stability | |
Hiromi Fukamachi2  Keiko Kobayashi2  Hiroshi Iijima1  Rika Satake-Ishikawa2  Katsuhiko Asano2  Haruhiko Tsumura2  Masaharu Ishikawa2  Akihiro Iwamatsu1  Shigeru Matsuki2  Toshihiko Kadoya2  Yoshihiro Shimada2  | |
[1] Central Laboratories for Key Technology, Kirin Brewery Co., Ltd.;Pharmaceutical Laboratory, Kirin Brewery Co., Ltd. | |
关键词: cysteine; granulocyte-colony stimulating factor; site-directed mutagenesis; thermostability; | |
DOI : 10.1247/csf.17.61 | |
学科分类:分子生物学,细胞生物学和基因 | |
来源: Japan Society for Cell Biology | |
【 摘 要 】
References(25)Cited-By(11)Human recombinant granulocyte-colony stimulating factor (rhG-CSF) has one free cysteine at position 17 and has two disulfide bridges (Cys36-Cys42 and Cys64-Cys74). The Cys17 of rhG-CSF was substituted with Gly, Ala, Ser, He, Tyr, Arg, and Pro, or deleted using site-directed mutagenesis in order to improve its thermostability. With the exception of Pro17-rhG-CSF, all mutant proteins retained biological activity which promotes the growth of mouse bone marrow cells in vitro. Amongthese mutant proteins, Ala17-rhG-CSF had more than 5 times higher stability than rhG-CSF. But Ser17-rhG-CSF had almost same stability as rhG-CSF and other mutant proteins had only lower stability.
【 授权许可】
Unknown
【 预 览 】
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