Abstract
TRNAPhe is able to elute phenylalanyl-tRNA synthetase from cation exchangers in a 1:1 ratio. Elution of phenylalanyl-tRNA synthetase in a 1:1 ratio is also observed for four noncognate tRNAs investigated, specific for valine, serine, isoleucine and tyrosine. If protein mixtures are subjected to affinity elution the cognate pair [tRNAPhe-phenylalanyl-tRNA synthetase] is eluted first, followed by noncognate pairs. The unspecific elution is not influenced by complexation of phenylalanyl-tRNA synthetase with an analog of phenylalanyl-adenylate.
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