A rapid and sensitive method to measure the enzymatic activity of ribosome-inactivating proteins | Zendy

Maurizio Brigotti | Zendy

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A rapid and sensitive method to measure the enzymatic activity of ribosome-inactivating proteins

Author(s) -

Maurizio Brigotti

Publication year - 1998

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/26.18.4306

Subject(s) - biology , ricin , ribosome inactivating protein , dna , biochemistry , purine , ribosome , microbiology and biotechnology , substrate (aquarium) , enzyme , plasmid , depurination , pbr322 , toxin , rna , ecology , gene

A method is described in which the adenosine- N -glycosidase activity of ribosome-inactivating proteins (RIPs) is measured using as substrate a 2251 bp [3H]DNA obtained by PCR amplification of the 731-2981 region of the pBR322 plasmid. The DNA, labelled in the purine ring of adenine, proved a good substrate for all three RIPs tested (PAP-S, ricin and shiga-like toxin I). The method, which measures directly the [3H]adenine released, is highly specific, extremely rapid and quantitative in a wide range of RIP concentrations.

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