Cell Structure and Function
Online ISSN : 1347-3700
Print ISSN : 0386-7196
ISSN-L : 0386-7196
The Substitution of Cysteine 17 of Recombinant HumanG-CSF with Alanine Greatly Enhanced its Stability
Masaharu Ishikawa, Hiroshi Iijima, Rika Satake-Ishikawa, Haruhiko Tsumura, Akihiro Iwamatsu, Toshihiko Kadoya, Yoshihiro Shimada, Hiromi Fukamachi, Keiko Kobayashi, Shigeru Matsuki, Katsuhiko Asano
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Keywords: cysteine, granulocyte-colony stimulating factor, site-directed mutagenesis, thermostability
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1992 Volume 17 Issue 1 Pages 61-65

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Abstract

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.

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© Japan Society for Cell Biology
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