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Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity

Paper ID Volume ID Publish Year Pages File Format Full-Text
25811 43603 2006 6 PDF Available
Title
Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity
Abstract

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).

Keywords
rhFGF-2; Mutation; Fluorescence spectroscopy; Mitogenic activityCD, circular dichroism; FGFR, fibroblast growth factor receptor; rhFGF-2M, mutant recombinant human fibroblast growth factor; rhFGF-2W, wild recombinant human fibroblast growth factor
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Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 121, Issue 4, 24 February 2006, Pages 442–447
Authors
, , , , , , , , , ,
Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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Any Questions? feel free to contact us