Mimicking of discontinuous epitopes by phage-displayed peptides, II. Selection of clones recognized by a protective monoclonal antibody against the Bordetella pertussis toxin from phage peptide libraries

Gene ◽  
1993 ◽  
Vol 128 (1) ◽  
pp. 21-27 ◽  
Author(s):  
Franco Felici ◽  
Alessandra Luzzago ◽  
Antonella Folgori ◽  
Riccardo Cortese
Keyword(s):  
Monoclonal Antibody ◽  
Pertussis Toxin ◽  
Bordetella Pertussis ◽  
Peptide Libraries ◽  
Bordetella Pertussis Toxin ◽  
Discontinuous Epitopes ◽  
Selection Of

Multiple species and isoforms of Bordetella pertussis toxin substrates

1988 ◽  
Vol 152 (3) ◽  
pp. 1185-1192 ◽  
Author(s):  
Philippe Brabet ◽  
Colette Pantaloni ◽  
Bruce Rouot ◽  
Madeleine Toutant ◽  
Adolfo Garcia-Sainz ◽  
...  
Keyword(s):  
Pertussis Toxin ◽  
Bordetella Pertussis ◽  
Bordetella Pertussis Toxin ◽  
Multiple Species

Comparison of real-time PCR and pyrosequencing for typing Bordetella pertussis toxin subunit 1 variants

2006 ◽  
Vol 65 (1) ◽  
pp. 153-158 ◽  
Author(s):  
Martin Storm ◽  
Abdolreza Advani ◽  
Monica Pettersson ◽  
Hans O. Hallander ◽  
Kåre Bondeson
Keyword(s):  
Real Time ◽  
Pertussis Toxin ◽  
Bordetella Pertussis ◽  
Real Time Pcr ◽  
Bordetella Pertussis Toxin

scholarly journals Effects of Bordetella pertussis toxin on catecholamine inhibition of insulin release from intact and electrically permeabilized rat islets

1989 ◽  
Vol 258 (3) ◽  
pp. 669-675 ◽  
Author(s):  
S J Persaud ◽  
P M Jones ◽  
S L Howell
Keyword(s):  
Molecular Mass ◽  
G Proteins ◽  
Insulin Release ◽  
Pertussis Toxin ◽  
Bordetella Pertussis ◽  
Pancreatic Beta Cells ◽  
Specific Binding ◽  
Rat Islets ◽  
Bordetella Pertussis Toxin

Noradrenaline- and clonidine-induced inhibition of insulin release from intact and electrically permeabilized rat islets was markedly relieved by prior exposure to 100 ng of Bordetella pertussis toxin/ml. The reversal of catecholamine inhibition of insulin secretion by this toxin was not associated with a decrease in specific binding of the alpha 2-adrenergic ligand [3H]yohimbine, and could not be fully explained by an increase in intracellular cyclic AMP. Exposure of intact islets to 1 microgram of pertussis toxin/ml for 2 h, followed by electrical permeabilization and incubation with 5 microCi of [alpha-32P]NAD+, resulted in the ADP-ribosylation in situ of a protein of molecular mass approx. 41 kDa. These results suggest that pertussis toxin alleviates catecholamine inhibition of beta-cell secretory responses by ADP-ribosylating at least one protein of molecular mass 41 kDa. In analogous systems the 41 kDa substrate of pertussis toxin has been shown to be the alpha subunit of Gi, but catecholamine-activated G proteins linked to effector systems other than adenylate cyclase might also be modified by this toxin in pancreatic beta-cells.

Rapid purification of Bordetella pertussis toxin by alternating affinity and hydrophobic chromatography

1986 ◽  
Vol 159 (2) ◽  
pp. 402-411 ◽  
Author(s):  
M. Svoboda ◽  
E. Hannecart-Pokorni ◽  
M. Borremans ◽  
J. Christophe
Keyword(s):  
Pertussis Toxin ◽  
Bordetella Pertussis ◽  
Hydrophobic Chromatography ◽  
Bordetella Pertussis Toxin ◽  
Rapid Purification
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