A RAPID HPLC DETERMINATION OF THE ISOMERIZATION LEVEL OF ASP-RESIDUES WITHIN SYNTHETICα-A-CRYSTALLIN FRAGMENTS

We describe a rapid HPLC method for measuring the isomerization levels of Asp-residues within peptides. This method can detect the isomerization of Asp-residue at a level of less than 1% without performance of acid hydrolysis. Using this method, we further studied the isomerization of Asp-residues i...

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Bibliographic Details
Published in:Journal of liquid chromatography & related technologies 2002-10, Vol.25 (16), p.2445-2454
Main Authors: Kaneda, Masaki, Nakagomi, Kazuya, Sadakane, Yutaka, Yamazaki, Toshiaki, Tanimura, Takenori, Akizawa, Toshifumi, Fujii, Noriko, Hatanaka, Yasumaru
Format: Article
Language:English
Subjects:
Aminoacids, peptides. Hormones. Neuropeptides
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Proteins
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Summary:We describe a rapid HPLC method for measuring the isomerization levels of Asp-residues within peptides. This method can detect the isomerization of Asp-residue at a level of less than 1% without performance of acid hydrolysis. Using this method, we further studied the isomerization of Asp-residues in the αA-crystallin f(55-65) fragment of sequence TVLDSGISEVR (T6). Four isomers of T6 peptides, which contain L-Asp, L-isoAsp, D-Asp, and D-isoAsp, respectively, were synthesized. Following incubation of any one of these peptides, four possible isomers of T6 peptides were found in an aqueous buffer. The isoAsp/ Asp ratios of peptides in these solutions were found to reach 3.6-3.8 after incubation at 90°C for 72 hr.
ISSN:1082-6076
1520-572X
DOI:10.1081/JLC-120014266