Biochemical properties of C78SC96S rhFGF-2: a double point-mutated rhFGF-2 increases obviously its activity.
Fibroblast growth factor-2 (FGF-2) is a multifunctional polypeptide that affects many cellular functions and phenomena. The wild-type recombinant human fibroblast growth factor rhFGF-2(W) and the mutant C78SC96S rhFGF-2(M) were expressed in Escherichia coli and their products were purified. The results by the means of fluorescence spectroscopy and CD spectrums, suggested that due to its decreased hydrophobicity rhFGF-2 is not deposited as an inclusion body. The mitogenic activity of the expressed rhFGF-2(M) on 3T3 fibroblasts was shown to be 10-fold more than the expressed rhFGF-2(W) of which the biological activity was a little less than that of the standard rhbFGF(W), indicating that the increased biological activity was due to the change of its secondary structure, dimerization and affinity binding to FGF receptor (FGFR).
Wang
Ju
J
Bio-Engineering Institute of Jinan University, Guangzhou 510632, PR China. wangju1688@163.com
Hong
An
A
Ren
Jin-Song
JS
Sun
Fen-Yong
FY
Shi
Ying-Jiao
YJ
Liu
Kan
K
Xie
Qiu-Ling
QL
Dai
Yun
Y
Li
Zhi-Ying
ZY
Chen
Yu
Y
D016475:3T3 Cells; D019943:Amino Acid Substitution; D000818:Animals; D049109:Cell Proliferation / Q000187:drug effects*; D016222:Fibroblast Growth Factor 2 / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D006801:Humans; D051379:Mice; D017354:Point Mutation; D017433:Protein Structure, Secondary / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D013329:Structure-Activity Relationship
D011994:Recombinant Proteins; D016222:Fibroblast Growth Factor 2