Oxidation of cysteine to cysteic acid in proteins by peroxyacids, as monitored by immobilized pH gradients
- 1 January 1991
- journal article
- research article
- Published by Wiley in Electrophoresis
- Vol. 12 (5), 376-377
- https://doi.org/10.1002/elps.1150120510
Abstract
It has often been debated whether the presence of persulfate in a polyacrylamide gel could lead to the oxidation of cysteine (Cys) in proteins to cysteic acid. In fact, direct incubation of bovine serum albumin (BSA) with peroxodisulfate and periodate barely alters the isoelectric point (pI) and does not produce any cysteic acid. In contrast, caroate (peroxomonosulfate) and perphathalate strongly lower the pI of BSA. In the former case it as demonstrated that 4‐ Cys (of a total of 35) were converted into cysteic acid. Perphthalate was found to be, by far, the strongest oxidant: 15 (of 35) Cys residues were oxidized to cysteic acid and all methionine groups were destroyed.Keywords
This publication has 6 references indexed in Scilit:
- Kinetics of cysteine oxidation in immobilized pH gradient gelsJournal of Chromatography A, 1990
- Carrier ampholyte-mediated oxidation of proteins in isoelectric focusingJournal of Chromatography A, 1989
- Charge heterogeneity of recombinant pro-urokinase and urinary urokinase, as revealed by isoelectric focusing in immobilized pH gradientsJournal of Chromatography A, 1989
- Enantioselective oxidation of sulphides by dioxiranes in the presence of bovine serum albuminTetrahedron Letters, 1989
- Postcolumn fluorometric detection system for liquid chromatographic analysis of amino and imino acids using o-phthalaldehyde/N-acetyl-l-cysteine reagentAnalytical Biochemistry, 1987
- Effect of isoelectric focusing on the amino-acid composition of proteinsThe Analyst, 1973