AI Article Synopsis
- A cellular enzyme transfers ADP-ribose from NAD to elongation factor 2 (EF-2), which inactivates EF-2 and inhibits protein synthesis in various animals and tissues.
- This enzyme's mechanism is similar to diphtheria toxin and Pseudomonas exotoxin A, but it only modifies a small portion of the EF-2 pool.
- Detection methods for the modified EF-2 include two-dimensional electrophoresis and immunoprecipitation, but the specifics of the cellular ADP-ribosyltransferase and its biological importance remain unclear.
Article Abstract
A cellular ADP-ribosyltransferase activity has been found in a variety of animals and tissues. The enzyme transfers ADP-ribose from NAD to elongation factor 2, inactivating the factor and thus inhibiting in vitro protein synthesis. Although, the mechanism of action of the cellular enzyme appears similar to diphtheria toxin and Pseudomonas exotoxin A, it differs from the toxins in that only a fraction of the EF-2 pool is modified. The endogenously ADP-ribosylated EF-2 has been detected by a variety of methods including two-dimensional electrophoresis and immunoprecipitation with elongation factor 2 antibody. The nature of the cellular ADP-ribosyltransferase and its physiological significance are unknown.
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| http://dx.doi.org/10.1007/BF00928454 | DOI Listing |
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