Quantification of Diphtheria Toxin–Mediated ADP-Ribosylation in a Solid-Phase Assay | Zendy

Christopher Bachran | Zendy; Mark Sutherland | Zendy; Diana Bachran | Zendy; Hendrik Fuchs | Zendy

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Quantification of Diphtheria Toxin–Mediated ADP-Ribosylation in a Solid-Phase Assay

Author(s) -

Christopher Bachran,

Mark Sutherland,

Diana Bachran,

Hendrik Fuchs

Publication year - 2007

Publication title -

clinical chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.705

H-Index - 218

eISSN - 1530-8561

pISSN - 0009-9147

DOI - 10.1373/clinchem.2007.085365

Subject(s) - adp ribosylation , biotinylation , diphtheria toxin , pertussis toxin , corynebacterium diphtheriae , cholera toxin , streptavidin , microbiology and biotechnology , chemistry , toxin , fusion protein , biochemistry , enzyme , diphtheria , recombinant dna , biology , biotin , nad+ kinase , g protein , virology , receptor , vaccination , gene

Because of reduced vaccination programs, the number of diphtheria infections has increased in the last decade. Diphtheria toxin (DT) is expressed by Corynebacterium diphtheriae and is responsible for the lethality of diphtheria. DT inhibits cellular protein synthesis by ADP-ribosylation of the eukaryotic elongation factor 2 (eEF2). No in vitro system for the quantification of DT enzymatic activity exists. We developed a solid-phase assay for the specific detection of ADP-ribosylation by DT.

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