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Mono-ADP-Ribosylation Catalyzed by Arginine-Specific ADP-Ribosyltransferases.
- Source :
-
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2018; Vol. 1813, pp. 149-165. - Publication Year :
- 2018
-
Abstract
- Methods are described for determination of arginine-specific mono-ADP-ribosyltransferase activity of purified proteins and intact cells by monitoring the transfer of ADP-ribose from NAD <superscript>+</superscript> to a model substrate, e.g., arginine, agmatine, and peptide (human neutrophil peptide-1 [HNP1]), and for the nonenzymatic hydrolysis of ADP-ribose-arginine to ornithine, a noncoded amino acid. In addition, preparation of purified ADP-ribosylarginine is included as a control substrate for ADP-ribosylation reactions.
- Subjects :
- ADP Ribose Transferases chemistry
ADP Ribose Transferases genetics
Adenosine Diphosphate Ribose analogs & derivatives
Adenosine Diphosphate Ribose chemistry
Adenosine Diphosphate Ribose genetics
Arginine chemistry
Catalysis
Humans
Ornithine chemistry
ADP Ribose Transferases isolation & purification
ADP-Ribosylation genetics
Adenosine Diphosphate Ribose isolation & purification
Molecular Biology methods
Subjects
Details
- Language :
- English
- ISSN :
- 1940-6029
- Volume :
- 1813
- Database :
- MEDLINE
- Journal :
- Methods in molecular biology (Clifton, N.J.)
- Publication Type :
- Academic Journal
- Accession number :
- 30097866
- Full Text :
- https://doi.org/10.1007/978-1-4939-8588-3_10