Arginyl-tRNA-protein transferase activities in crude supernatants of rat tissues

A fluorescent HPLC method for the assay of arginyl-tRNA-protein transferase (R-Transferase) activity was applied to obtain quantitative data of the en zyme activity in rat tissues for the first time. In this assay, the major p roblem was a significant hydrolysis of the substrate, N-aspartyl-N'-dansyla mido-1,4-butanediamine, and the product, N-arginylaspartyl-N'-dansylamido-1 ,4-butanediamine (ArgAsp(4)DNS) by aminopeptidases in crude samples such as 105000 g supernatants (105S) of tissue homogenates. As bestatin inhibited the hydrolysis of ArgAsp(4)DNS, a standard-addition method in the presence of bestatin, using a partially purified R-Transferase preparation from hog kidney as a standard, made it possible to measure directly R-Transferase ac tivities in 105S with a short incubation time and sufficient reliability. I t was found by the established method that of 14 tissues examined, stomach was rich in the R-Transferase activity with the highest specific activity, suggesting a target tissue for the future studies on R-Transferase to eluci date its physiological significance.