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Bovine factor VII. Its purification and complete amino acid sequence
H Takeya1, S Kawabata, K Nakagawa
1Department of Biology, Faculty of Science, Kyushu University, Fukuoka, Japan.
The Journal of Biological Chemistry
|October 15, 1988
Summary
Researchers purified bovine blood clotting factor VII and determined its complete amino acid sequence. This bovine factor VII shows high sequence identity with the human molecule, aiding comparative studies.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Blood clotting factor VII is crucial for hemostasis.
- Understanding factor VII structure aids in developing targeted therapies.
Purpose of the Study:
- To develop a modified purification method for bovine blood clotting factor VII.
- To establish the complete amino acid sequence of bovine factor VII.
Main Methods:
- Purification of bovine factor VII from plasma.
- Activation with factor XIIa, reduction, and S-alkylation (S-pyridylethylation or S-aminoethylation).
- Amino acid sequencing of heavy and light chains using enzymatic/chemical cleavage and mass spectrometry.
Main Results:
- Complete amino acid sequence of bovine factor VII (407 residues) established.
- Light chain (152 residues) contains glycosylation and gamma-carboxyglutamic acid residues.
- Heavy chain (255 residues) contains a glycosylation site.
- Bovine factor VII exhibits 71% sequence identity with human factor VII.
Conclusions:
- The study provides the complete amino acid sequence of bovine factor VII.
- Identified post-translational modifications including glycosylation and gamma-carboxylation.
- High sequence homology suggests conserved function between bovine and human factor VII.
