Journal of Analytical & Bioanalytical Techniques
Open Access

Review Article

Current Methods for Analysis of Enzymatic Peptidyl-tRNA Hydrolysis

Department of Chemistry, University of Alabama in Huntsville, USA

*Corresponding Author:

Dr. Robert L McFeeters
Associate Professor, Department of Chemistry
University of Alabama in Huntsville
301 Sparkman Dr, Huntsville, AL 35899, USA
Tel: (256) 824-6023
Fax: (256) 824-6349
E-mail: robert.mcfeeters@uah.edu

Received date: September 15, 2014; Accepted date: October 28 2014; Published date: October 31, 2014

Citation: McFeeters H, McFeeters RL (2014) Current Methods for Analysis of Enzymatic Peptidyl-tRNA Hydrolysis. J Anal Bioanal Tech 5:215. doi: 10.4172/2155-9872.1000215

Copyright: © 2014 McFeeters H, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Understanding peptidyl-tRNA and the enzymes responsible for recycling them has come from the ability to detect and quantify enzymatic peptidyl-tRNA hydrolysis. The methods available to study removal of peptides from tRNA have evolved considerably. Radioactive [14C] amino acids were first implemented to monitor cleavage of the peptide-nucleotide ester bond of uniform peptidyl-tRNA substrates. Later, Northern blots with radiolabeled oligonucleotide probes were used to observe cleavage of specific peptidyl-tRNAs or individual tRNA from bulk peptidyl-tRNA populations. Finally, the use of fluorescently labeled amino acids was introduced, which could be coupled to anisotropy or PAGE readouts. Here we review the methods for quantification and analysis of enzymatic peptidyl-tRNA hydrolysis and summarize their inherent advantages and disadvantages.

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