Optimal conditions for the use of protein l-isoaspartyl methyltransferase in assessing the isoaspartate content of peptides and proteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference33 articles.
1. Partial repair of deamidation-damaged calmodulin by protein carboxyl methyltransferase.
2. Formation of Isoaspartate at Two Distinct Sites during in vitro Aging of Human Growth Hormone
3. Deamidation of calmodulin at neutral and alkaline pH: Quantitative relationships between ammonia loss and the susceptibility of calmodulin to modification by protein carboxyl methyltransferase
4. Calcium affects the spontaneous degradation of aspartyl/asparaginyl residues in calmodulin
5. Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25. Evidence for methylation at the alpha-carboxyl group of atypical L-isoaspartyl residues.
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