Even if you got some tRNA with still-attached amino acids out of your preparation, you certainly would have a mixture of free and loaded tRNAs (probably more free tRNA). Therefore, the only way to get aa-loaded tRNA is to make a tRNA prep and subsequently perform in-vitro loading with amino acids. I f you do that with a 100.000 g supernatant of cell extract (source of the tRNA-synthetases), crude tRNA prep, ATP and only the one amino acid of your choice, you end up with a mixture of all tRNAs, but only the one you wanted loaded with amino acid. If you need pure tRNA-Met, you either have go through a complicated purification procedure based on column chromatographic steps or similar techniques to purifiy the tRNA species you want from all of the others (if you need it with all the modified bases), or you can try to generate a pure RNA construct (without modifications) by in-vitro run-off transcription of the gene cloned into an appropriate T7-promotor vector using phage T7 RNA polymerase. In either case, you need to charge the tRNA again with the amino acid in-vitro.

Thank you for you reply. I don't need a pure tRNA-Met, I just need a good portion of it in a total RNA extraction. I plan on digesting the RNA with RNase. The end goal is to know that the methionine in the solution after RNase treatment came from tRNA and not other sources (protein cleavage etc.)

I can't find the right protocol at the moment and will post it later.

The only important thing I remember is to work under slightly acidic conditions (pH ~ 4-5) in order to maintain the tRNA aminoacylated. I am not sure what the pH  of TRIZOL reagent is but it may not be suitable for that purpose.

You will have a problem with this analysis. You can not expect even with the best method of purifying tRNA that you get completely rid of any proteins or free methionine. Therefore, you can never be sure whether the Met you recover from your tRNA fraction is actually from charged tRNA or other sources (this would also be my judgement if I had to review a paper claiming this). In my opinion, you only can make sure that you are looking at tRNA-bound Met if you analyse for the amino acid still bound to the last nucleotide of the tRNA (e.g. the adenosyl-Met you would expect from the 3'-side A of fully cleaved tRNA  ore something like CCA-Met from partially cleaved tRNA after RNase treatment. You should also think of setting this up as radiolabeled assay (e.g. 35S-Met) to gain the necessary analytic sensitivity for picking up the signals in a lot of background molecules. In terms of RNA preparartion, your goal calls for a methods that works under acidic conditions (best stability of charged tRNAs) and is fast in inactivating RNases and allowing only a short time for hydrolysing the amino acid off the tRNA.

A better way of analysing the amonunt of met loaded on total tRNA may be to adapt the "native" polyacrylamide gel separation of charged tRNA established by U. RajBhandari (again best with 35-S label) and quantify the band-shifted labeled form of tRNA-met.