Availability of DNP-modified 5'- and 3'-ends of the poly(U) fragment bound to the 30S ribosomal subunit for interaction with antibodies

Modification of the 5'- or 3'-terminal nucleotide residues of poly(U) by dinitrophenyl haptens was carried out. The accessibility of the modified ends of short poly(U) (20-70 nucleotide residues) bound to the 30S subunit of E. coli ribosomes for the interaction with antibodies that are spe...

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Bibliographic Details
Published in:	Biokhimiia (Moscow, Russia) Vol. 49; no. 7; p. 1059
Main Authors:	Evstaf'eva, A G, Shatskiĭ, I N
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-07-1984
Subjects:	Antibodies - immunology Antibodies - metabolism Base Composition Binding Sites, Antibody Dinitrobenzenes - immunology Dinitrobenzenes - pharmacology Haptens - immunology Haptens - pharmacology Hydrolysis Nitrobenzenes - pharmacology Poly U - immunology Poly U - metabolism Ribosomes - immunology Ribosomes - metabolism RNA, Transfer, Amino Acyl - metabolism Templates, Genetic
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Summary:	Modification of the 5'- or 3'-terminal nucleotide residues of poly(U) by dinitrophenyl haptens was carried out. The accessibility of the modified ends of short poly(U) (20-70 nucleotide residues) bound to the 30S subunit of E. coli ribosomes for the interaction with antibodies that are specific against the dinitrophenyl group, was investigated. Some peculiarities of the structural organization of the "entry" (3'-end) and "exit" (5'-end) sites of the template polynucleotide on the 30S subunit and the possibility of the template polynucleotide folding on the ribosome are discussed.
ISSN:	0320-9725