Biochemical and Biophysical Research Communications
Stabilizing basic fibroblast growth factor using protein engineering
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Separation of truncated basic fibroblast growth factor from the full-length protein by hydrophobic interaction chromatography
2021, Separation and Purification TechnologyCitation Excerpt :Human FGF-2 has a size of 17 kD and is a protein with an extremely alkaline pI of 9.6. When FGF-2 is stored over time, it starts to form aggregates or to degrade [2–8], which can be a challenge during manufacturing to gain the full-length protein without product related impurities. Its chemical instability is commonly associated with the presence of four cysteines in the primary sequence of this protein but no intramolecular disulfide bond is present in the native FGF-2.
Leukocyte cell-derived chemotaxin 2 is a zinc-binding protein
2013, FEBS LettersCitation Excerpt :Therefore only a small number of residual cysteine residues that did not form the disulfide bonds were available to participate in this reaction. It is known that oligomerization of a recombinant protein is occasionally caused by oxidation [23,24]. On the other hand, it is possible that another structural property of LECT2 caused the oligomerization, as in the case of β2-microglobulin [25].
A multi-step method for preparation of porcine small intestinal submucosa (SIS)
2011, BiomaterialsCitation Excerpt :Compared to SISi treated with the mechanical method, the content of TGF-β decreased to 28.7%, the content of b-FGF to 54.2%, VEGF to 36.39%, and TNF-α to 61.64% in SISv, implied that b-FGF and TNF-α may be inherently more stable than other growth factors. A previous study showed that b-FGF can retain its activity under acidic and oxidizing conditions, even if absent of stabilizing agents [49]. In our in vivo experiment, SISi and SISv were transplanted subcutaneously into SD rats and the tissues were examined at 1, 2, and 4 weeks, respectively.
Generation of highly stable IL-18 based on a ligand-receptor complex structure
2004, Biochemical and Biophysical Research CommunicationsCitation Excerpt :To obtain an antioxidative stable hIL-18, we conservatively mutated all the cysteine residues to serine; and as the 3D-structure analyses predicted (Fig. 3), the resulting mutant protein, IL-18-AS, showed high stability retaining biological activity even after oxidation (Fig. 6). In human fibroblast growth factor (hFGF), replacement of two of the four cysteine residues by serine (C70S and C88S) could improve instability; retaining the biological activities, but replaced the other two cysteine residues (C26S and C93S) resulting in a marked reduction in activity [16,17]. Biochemical analyses suggested that two cysteine residues (C26 and C93) form an intramolecular disulfide bond [17].
Fibroblast growth factor inhibits locomotor activity as well as feeding behavior of rats
2001, European Journal of PharmacologyDistinct signaling pathways involved in multiple effects of basic fibroblast growth factor on cultured rat hippocampal neurons
2000, Brain ResearchCitation Excerpt :P values less than 0.05 were considered significant. bFGF used in this study is CS23, a modified human bFGF in which serine is substituted for cysteine at amino acid residues 70–88 to prevent conformational changes and increase stability [1,26]. Calphostin C was a generous gift from Kyowa Hakko Kogyo Ltd.