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Hydrolyse des aminoacyl‐tARN par la phosphodiesterase du venin
Author(s) -
Yot P.,
Gueguen P.,
Chapeville F.
Publication year - 1968
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(68)80046-8
Subject(s) - chemistry , hydrolysis , lysine , phosphodiesterase , amino acid , aminoacyl trna , dipeptide , glutamic acid , biochemistry , enzyme , transfer rna , rna , gene
The influence of the esterification of the 3′(2′) hydroxyl group of tRNA on the hydrolysis by venom phosphodiesterase ( Crotalus adamanteus ) was studied. It was shown that this esterification does not change the rate of hydrolysis. At pH 7–8, no significant differences were observed either when the α amino group of the attached amino acid was free or blocked, or when the aminoacid contained a free carboxyl group or a second amino group (glutamic acid or lysine). Aminoacyl‐AMP or oligopeptidyl‐AMP can be prepared by this method.