Expression of the S-1 catalytic subunit of pertussis toxin in Escherichia coli.
AUTOR(ES)
Barbieri, J T
RESUMO
The S-1 subunit of pertussis toxin was expressed as a fusion protein in a strain of Escherichia coli deficient in protein degradation. The fusion protein reacted with anti-pertussis toxin antibody, and, like authentic pertussis toxin, it ADP-ribosylated a 41,000-molecular-weight membrane protein from human erythrocytes.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=260508Documentos Relacionados
- Expression and secretion of the S-1 subunit and C180 peptide of pertussis toxin in Escherichia coli.
- ADP-ribosyltransferase mutations in the catalytic S-1 subunit of pertussis toxin.
- Photolabeling of Glu-129 of the S-1 subunit of pertussis toxin with NAD.
- Activities of complete and truncated forms of pertussis toxin subunits S1 and S2 synthesized by Escherichia coli.
- Membrane Localization of the S1 Subunit of Pertussis Toxin in Bordetella pertussis and Implications for Pertussis Toxin Secretion
