"Half-site" affinity modification of tryptophanyl-tRNA synthetase leads to "freezing" of the free subunit.

Favorova, O O; Madoyan, I A; Drutsa, V L

Favorova, O O; Madoyan, I A; Drutsa, V L.

FEBS Lett ; 123(2): 161-4, 1981 Jan 26.

Article in En | MEDLINE | ID: mdl-6262106

Subject(s)

Adenosine Monophosphate/analogs & derivatives; Affinity Labels/pharmacology; Amino Acyl-tRNA Synthetases/antagonists & inhibitors; Tryptophan-tRNA Ligase/antagonists & inhibitors; Adenosine Monophosphate/metabolism; Adenosine Monophosphate/pharmacology; Adenosine Triphosphate/metabolism; Animals; Binding Sites/drug effects; Cattle; Diphosphates/metabolism; Kinetics; Macromolecular Substances; Pancreas/enzymology; Tryptophan/analogs & derivatives; Tryptophan/metabolism; Tryptophan-tRNA Ligase/metabolism

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Database: MEDLINE Main subject: Tryptophan-tRNA Ligase / Affinity Labels / Adenosine Monophosphate / Amino Acyl-tRNA Synthetases Limits: Animals Language: En Journal: FEBS Lett Year: 1981 Type: Article

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