Aminoacylation of rat liver transfer RNA with L-penicillamine. On the specificity of the aminoacylation reaction.
Biochim Biophys Acta
; 474(2): 210-7, 1977 Jan 20.
Article
en En
| MEDLINE
| ID: mdl-318863
ABSTRACT
L-]14C]Penicillamine is bound to RNA from rat liver in an in vitro reaction catalyzed by rat liver aminoacyl-tRNA synthetases. Addition of certain naturally occuring amino acids results in a significant decrease of L-penicillamine binding. The most potent inhibitor of this binding is L-valine, followed by L-isoleucine and L-threonine. Amino acids without structural relationship to L-penicillamine in the non-functional part of the molecule, such as L-phenylalanine, are ineffective. Studies on the competition of L-penicillamine and L-isoleucine, respectively, with L-valine demonstrate the high specificity of the aminoacylation reaction. They show that the change of L-penicillamine binding to tRNA Val is considerably lower than that of L-valine.
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Bases de datos:
MEDLINE
Asunto principal:
Penicilamina
/
ARN de Transferencia
/
Aminoacil-ARNt Sintetasas
/
Hígado
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1977
Tipo del documento:
Article