Purification of the sodium transport enzyme oxaloacetate decarboxylase by affinity chromatography on avidin sepharose |
| |
Authors: | Peter Dimroth |
| |
Institution: | Institut für Physiologische Chemie der Technischen Universität München, Biedersteiner Straße 29, 8000 München 40, FRG |
| |
Abstract: | 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. The linkage between aspartic acid and the protein is acid and alkali resistant; thus it is likely a peptide-like amide bond formed between the activated carboxylate group of aspartic acid and the primary amine function of the side chain of lysine residues. |
| |
Keywords: | To whom correspondence should be addressed |
本文献已被 ScienceDirect 等数据库收录! |
|