Add time:08/17/2019         Source:sciencedirect.com

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 tRNAVal is considerably lower than that of l-valine.

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