Human brain fibroblast growth factor. Isolation and partial chemical characterization

Area of Science:

• Biochemistry
• Molecular Biology
• Cell Biology

Background:

• Fibroblast growth factor (FGF) is a key signaling protein involved in cell proliferation and differentiation.
• Understanding the structure and function of FGF from different sources is crucial for biomedical research.

Purpose of the Study:

• To purify human brain fibroblast growth factor (FGF) to homogeneity.
• To determine the amino-terminal sequence of human brain FGF.
• To compare the structure of human brain FGF with that of bovine FGF.

Main Methods:

• Protein purification involving salt precipitation, cation-exchange chromatography, Heparin-Sepharose affinity chromatography, and reverse-phase HPLC.
• Monitoring isolation using radioimmunoassay and in vitro vascular endothelial cell proliferation assays.
• Amino-terminal sequencing using Edman degradation.

Main Results:

• Human brain FGF was successfully purified to homogeneity.
• The amino-terminal sequence of human brain FGF was determined as Pro-Ala-Leu-Pro-Glu-Asp-Gly-Gly-Ser-Gly-Ala-Phe-Pro-.
• This sequence was found to be identical to the amino-terminal sequence of bovine FGF.

Conclusions:

• Human brain FGF is structurally very similar to bovine FGF, based on identical amino-terminal sequences.
• The purification and characterization of human brain FGF provide insights into its biological roles.
• These findings suggest conserved structural features of FGF across mammalian species.