DNA sequence coding for the complete human C3a with 77 amino acids was divided into three portions, synthesized separately and constructed for expression in Escherichia coli. High expression of the recombinant C3a was achieved by an expression system using T7 polymerase. Purified recombinant C3a showed the same activities of ileum contraction and platelet aggregation of guinea pig as C3a purified from human serum.
|Number of pages||8|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - 1991 Mar 29|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology