Attachment of protein affinity-labeling reagents of variable length and amino acid specificity to E. coli tRNAfMet.

AUTOR(ES)

Schulman, L H

RESUMO

Transamination with bifunctional amines in the presence of bisulfite has been used to attach side chains of variable length to the N4-position of single stranded cytidine residues in E. coli tRNAfMet. Such side chains, terminating in reactive primary amino groups, have been coupled to a variety of N-hydroxysuccinimide esters. The resulting modified tRNAs carry protein affinity labeling groups capable of covalent reaction with a variety of amino acids.

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