Journal article
Method of analysis of recombinant acidic fibroblast growth factor by capillary electrophoresis
Journal of chromatography. B, Biomedical sciences and applications, v 695(1), pp 49-58
18 Jul 1997
PMID: 9271128
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Fibroblast growth factors are a series of well characterized proteins that have intriguing pharmacological properties. Acidic fibroblast growth factor (aFGF) recently appeared in the literature for its efficacy in spinal cord repair in rats. The protein has proven difficult to analyze by capillary electrophoresis, because it has a tendency to unfold, aggregate and precipitate, especially near and above physiological temperatures. By studying the turbidity of capillary electrophoresis running buffers and aFGF at 50 degrees C, conditions were found that stabilize the aFGF solution, thereby allowing the capillary electrophoretic separation of the protein from its recombinant production impurities. The buffer system employs 50 mM phosphate buffer at pH 2.5 with 0.25% hydroxypropylmethylcellulose (HPMC) additive. This system provided the best efficiency and selectivity of the systems studied and was developed for pharmaceutical purity analysis.
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Details
- Title
- Method of analysis of recombinant acidic fibroblast growth factor by capillary electrophoresis
- Creators
- T P Roddy - Department of Chemistry, Villanova University, PA 19085, USAT E MolnarR E McKeanJ P Foley
- Publication Details
- Journal of chromatography. B, Biomedical sciences and applications, v 695(1), pp 49-58
- Publisher
- Elsevier; Netherlands
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:A1997XN72300006
- Scopus ID
- 2-s2.0-0030750264
- Other Identifier
- 991014877935204721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemical Research Methods
- Chemistry, Analytical