Aspartyl-tRNA Synthetase-Induced Aspartylation of Proteins: a Fingerprint Approach to Map Accessible Domains in Protein
Aspartic acid can be covalently linked to yeast aspartyl-tRNA synthetase and to other proteins in the absence of tRNA, under conditions where the synthetase activates the amino acid into aspartyl-adenylate, i.e., in the presence of ATP and MgCl2 [1,2]. The aspartyl adenylate is poorly bound to the enzyme.
KeywordsHPLC Serine Lysine Ketone Trypsin
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