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Transforming growth factor e: amino acid analysis and partial amino acid sequence
P G Parnell1, J Wunderlich, B Carter
1Department of Pathology, College of Veterinary Medicine, University of Georgia, Athens 30602.
Growth Factors (Chur, Switzerland)
|January 1, 1992
Summary
Transforming growth factor epsilon (TGFe) was purified to homogeneity from bovine kidney. This growth factor promotes epithelial and fibroblastic cell proliferation and shows no similarity to other known growth factors.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Transforming growth factor epsilon (TGFe) is a known mitogen for epithelial and fibroblastic cells.
- TGFe has been identified in various normal and neoplastic tissues, as well as body fluids.
Purpose of the Study:
- To purify TGFe to homogeneity from bovine kidney.
- To characterize the amino acid composition and partial sequence of purified TGFe.
Main Methods:
- Multistep purification protocol from bovine kidney.
- High-performance electrophoresis chromatography as the final purification step.
- Amino acid analysis and partial amino acid sequencing of purified TGFe.
Main Results:
- TGFe was successfully purified to homogeneity.
- Amino acid analysis revealed a high content of proline, aspartate, and glutamate.
- Partial amino acid sequencing showed no similarity to other characterized growth factors.
Conclusions:
- TGFe is a distinct growth factor with a unique amino acid profile.
- The purification and characterization of TGFe provide a foundation for further functional studies.