Results 171 to 180 of about 51,446 (212)

The crystal structure of pertussis toxin [PDF]

Structure, 1994
Pertussis toxin is an exotoxin of the A-B class produced by Bordetella pertussis. The holotoxin comprises 952 residues forming six subunits (five different sequences, S1-S5). It plays an important role in the development of protective immunity to whooping cough, and is an essential component of new acellular vaccines.
Randy J Read
exaly   +3 more sources

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Pertussis toxin (Bordetella pertussis)

1997
Abstract PT (Sekura et al. 1985) is a protein of 105 000 daltons composed of five noncovalently linked subunits named 51 through 55, and organized into two functional domains called A and B (Tamura et al. 1982). The A domain, which is composed of the 51 subunit, is an enzyme that intoxicates eukaryotic cells by ADP-ribosylating their GTP¬
R Rappuoli, M G Pizza
openaire   +1 more source

The pertussis toxin liberation genes of Bordetella pertussis are transcriptionally linked to the pertussis toxin operon

Infection and Immunity, 1996
The DNA sequence of the pertussis toxin operon (ptx) of Bordetella pertussis predicts that transcription of the operon ends downstream from the ptxS3 gene at a possible stem-loop structure. Secretion of the assembled pertussis toxin into the culture medium required the expression of 8 genes arranged in an operon (ptl) and lying 55 bp downstream from ...
Ricci S., Rappuoli R., Scarlato V.
openaire   +3 more sources

Binding of NAD+ to pertussis toxin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
The equilibrium dissociation constant of NAD+ and pertussis toxin was determined by equilibrium dialysis and by the quenching of the protein's intrinsic fluorescence on titration with NAD+. A binding constant, Kd, of 24 +/- 2 microM at 30 degrees C was obtained from equilibrium dialysis, consistent with the previously determined value for the Michaelis
M D, Lobban, L I, Irons, S, van Heyningen   +2 more
openaire   +2 more sources

The effect of pH on the production of pertussis toxin by Bordetella pertussis

Journal of Biotechnology, 1991
The production of pertussis toxin by Bordetella pertussis was increased by controlling the pH at 7.0 through the addition of sulfuric acid. The more commonly used hydrochloric acid and Tris buffer were observed to be detrimental to toxin yields.
P, Licari, L, Winberry, R, Swartz
openaire   +2 more sources

The role of pertussis toxin in clinical manifestations of pertussis

Toxicon
Pertussis is an acute respiratory infectious disease caused by Bordetella pertussis (B. pertussis). In recent years, the resurgence of pertussis has once again drawn widespread attention from the academic community and society at large. The pathogenicity of B.
Wenjuan, Zhao, Meng, Dang, Shuyue, Tang, Min, Hao, Zengguo, Wang   +4 more
openaire   +2 more sources

Production of cell mass and pertussis toxin by Bordetella pertussis

Journal of Biotechnology, 1991
The cultivation of Bordetella pertussis affects production of pertussis toxin and biomass. Comparison of batch mode, chemostat operation and pHstat-turbidostatic control showed that productivities for the continuous process were greater than that for the batch operation.
P, Licari, G R, Siber, R, Swartz
exaly   +3 more sources

Binding of ATP by pertussis toxin and isolated toxin subunits

Biochemistry, 1990
The binding of ATP to pertussis toxin and its components, the A subunit and B oligomer, was investigated. Whereas, radiolabeled ATP bound to the B oligomer and pertussis toxin, no binding to the A subunit was observed. The binding of [3H]ATP to pertussis toxin and the B oligomer was inhibited by nucleotides.
S Z, Hausman, C R, Manclark, D L, Burns
openaire   +2 more sources

Bordetella pertussis toxins

Pharmacology & Therapeutics, 1982
A C, Wardlaw, R, Parton
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Pertussis Toxin

2006
  +4 more sources