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Primary structure of ovine pituitary basic fibroblast growth factor
R J Simpson1, R L Moritz, C J Lloyd
1Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research (Melbourne), Victoria, Australia.
FEBS Letters
|November 16, 1987
Summary
Researchers determined the full amino acid sequence of ovine basic fibroblast growth factor (FGF). This sequence analysis revealed minor differences compared to bovine and human basic FGF, aiding in understanding protein evolution.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Chemistry
Background:
- Basic fibroblast growth factor (FGF) is crucial for cellular processes.
- Understanding FGF sequence variations across species is important for comparative biology.
Purpose of the Study:
- To establish the complete amino acid sequence of basic FGF from ovine pituitary glands.
- To compare the ovine basic FGF sequence with its bovine and human counterparts.
Main Methods:
- Sequence analysis of intact ovine basic FGF and derived peptides.
- Enzymatic digestion using clostripain, chymotrypsin, pepsin, and S. aureus V8 protease.
- Purification and isolation of peptides using microbore HPLC and ion-pairing chromatography.
Main Results:
- The complete 146-residue amino acid sequence of ovine basic FGF was determined.
- Ovine basic FGF differs from bovine basic FGF by one positional amino acid residue.
- Ovine basic FGF differs from human basic FGF by three positional amino acid residues.
Conclusions:
- The study provides the definitive amino acid sequence for ovine basic FGF.
- Identified sequence variations highlight evolutionary divergence between ovine, bovine, and human basic FGFs.