کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
25811 | 43603 | 2006 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity](/preview/png/25811.png)
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-2W and the mutant C78SC96S rhFGF-2M 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-2M on 3T3 fibroblasts was shown to be 10-fold more than the expressed rhFGF-2W of which the biological activity was a little less than that of the standard rhbFGFW, indicating that the increased biological activity was due to the change of its secondary structure, dimerization and affinity binding to FGF receptor (FGFR).
Journal: Journal of Biotechnology - Volume 121, Issue 4, 24 February 2006, Pages 442–447