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Fibroblast growth factor in the human placenta
Biochemical and Biophysical Research Communications
|April 30, 1985
Summary
Human placenta fibroblast growth factor (FGF) was purified using advanced chromatography. This purified FGF is biologically similar to bovine pituitary FGF, suggesting a close molecular relationship between species.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Fibroblast growth factor (FGF) plays a crucial role in cellular processes.
- Understanding FGF structure and function is vital for biological research.
Purpose of the Study:
- To purify and characterize fibroblast growth factor (FGF) from human placenta.
- To compare human placental FGF with bovine pituitary FGF.
Main Methods:
- Purification involved salt precipitation, cation-exchange chromatography, and Heparin-Sepharose affinity chromatography.
- Characterization included molecular weight determination, amino acid composition analysis, bioactivity assays, and immunological crossreactivity tests.
Main Results:
- FGF was purified 333,000-fold from human placenta.
- The purified human FGF has a molecular weight of 15-16 kDaltons.
- Human placental FGF demonstrated bioactivity and immunological crossreactivity similar to bovine pituitary FGF.
Conclusions:
- Human placenta is a viable source for FGF purification.
- Human placental FGF and bovine pituitary FGF are closely related molecules.
- These findings contribute to the understanding of FGF's conserved structure and function across species.