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Nucleic Acids Research, 1981, Vol. 9, No. 5 1203-1217
© 1981

CHEMISTRY

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

LaDonne H. Schulman, Heike Pelka and Scott A. Reines

Department of Developmental Biology and Cancer, Division of Biology, Albert Einstein College of Medicine Bronx, NY 10461, USA

Received January 21, 1981. 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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