Active recombinant C3a of human anaphylatoxin produced in Escherichia coli.
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.
Fukuoka
Y
Y
Department of Immunology, Tohoku University, Sendai, Japan.
Yasui
A
A
Tachibana
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D015926:Complement C3a / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification / Q000494:pharmacology; D004247:DNA / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics*; D006168:Guinea Pigs; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000187:drug effects; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D010974:Platelet Aggregation / Q000187:drug effects; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000494:pharmacology; D015183:Restriction Mapping
D011994:Recombinant Proteins; D015926:Complement C3a; D004247:DNA