Quantification of the isomerization of Asp residue in recombinant human αA-crystallin by reversed-phase HPLC
- 15 January 2003
- journal article
- Published by Elsevier BV in Journal of Pharmaceutical and Biomedical Analysis
- Vol. 30 (6), 1825-1833
- https://doi.org/10.1016/s0731-7085(02)00525-3
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 27 references indexed in Scilit:
- A RAPID HPLC DETERMINATION OF THE ISOMERIZATION LEVEL OF ASP-RESIDUES WITHIN SYNTHETIC?-A-CRYSTALLIN FRAGMENTSJournal of Liquid Chromatography & Related Technologies, 2002
- Limited Accumulation of Damaged Proteins inl-Isoaspartyl (d-Aspartyl)O-Methyltransferase-deficient MicePublished by Elsevier BV ,2001
- d-Amino Acid Formation Induced by a Chiral Field within a Human Lens Protein during AgingBiochemical and Biophysical Research Communications, 1999
- Cloning, Expression, and Chaperone-like Activity of Human αA-CrystallinPublished by Elsevier BV ,1996
- Simultaneous racemization and isomerization at specific aspartic acid residues in αB-crystallin from the aged human lensBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
- Comparison of separation and detection techniques for human growth hormone releasing factor (hGRF) and the products derived from deamidationJournal of Pharmaceutical and Biomedical Analysis, 1993
- Identification and quantitation of tetrapeptide deamidation products by mass spectrometryJournal of Pharmaceutical and Biomedical Analysis, 1992
- Site‐specific racemization in aging α‐crystallinFEBS Letters, 1990
- In vivo processing of N‐terminal methionine in E. coliFEBS Letters, 1990
- Aspartic acid racemisation in the human lens during ageing and in cataract formationNature, 1977