Abstract
This work indicates that free methylated albumin (MA) can form a precipitable complex with tRNA under a variety of conditions. This complex renders the tRNA reversibly inactive in accepting amino acids, non-exchangeable with free aminoacyl-tRNA in solution, and partially resistant to RNAse. The stability of the complex is partially salt-dependent and shows some ion-specificity. Urea has little effect on complex formation or dissociation. Pretreatment of the complex with pronase, followed by phenol leads to total recovery of amino acid acceptor activity of the tRNAs. Phenol treatment alone does not. No interaction between the synthetase enzymes and MA could be detected.
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