PL EN


Preferences help
enabled [disable] Abstract
Number of results
2001 | 48 | 1 | 271-275
Article title

Chlorination of N-acetyltyrosine with HOCl, chloramines, and myeloperoxidase-hydrogen peroxide-chloride system

Content
Title variants
Languages of publication
EN
Abstracts
EN
N-acetyl-L-tyrosine (N-acTyr), with the alpha amine residue blocked by acetylation, can mimic the reactivity of exposed tyrosyl residues incorporated into polypeptides. In this study chlorination of N-acTyr residue at positions 3 and 5 in reactions with NaOCl, chloramines and the myeloperoxidase (MPO)-H2O2-Cl- chlorinating system were invesigated. The reaction of N-acTyr with HOCl/OCl- depends on the reactant concentration ratio employed. At the OCl-/N-acTyr (molar) ratio 1:4 and pH 5.0 the chlorination reaction yield is about 96% and 3-chlorotyrosine is the predominant reaction product. At the OCl-/ N-acTyr molar ratio 1:1.1 both 3-chlorotyrosine and 3,5-dichlorotyrosine are formed. The yield of tyrosine chlorination depends also on pH, amounting to 100% at pH 5.5, 91% at pH 4.5 and 66% at pH 3.0. Replacing HOCl/OCl- by leucine/chloramine or alanine/chloramine in the reaction system, at pH 4.5 and 7.4, produces trace amount of 3-chlorotyrosine with the reaction yield of about 2% only. Employing the MPO-H2O2-Cl- chlorinating system at pH 5.4, production of a small amount of N-acTyr 3-chloroderivative was observed, but the reaction yield was low due to the rapid inactivation of MPO in the reaction system. The study results indicate that direct chlorination of tyrosyl residues which are not incorporated into the polypeptide structure occurs with excess HOCl/OCl- in acidic media. Due to the inability of the myeloperoxidase-H2O2-Cl- system to produce high enough HOCl concentrations, the MPO-mediated tyrosyl residue chlorination is not effective. Semistable amino-acid chloramines also appeared not effective as chlorine donors in direct tyrosyl chlorination.
Publisher

Year
Volume
48
Issue
1
Pages
271-275
Physical description
Dates
published
2001
received
2000-03-13
revised
2000-11-30
accepted
2001-02-27
Contributors
  • Department of Diagnostics and Chair of Clinical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
  • Department of Diagnostics and Chair of Clinical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
References
  • Domingan, N.M., Charlton, T.S., Duncan, M.W., Winterburn, C.C. & Kettle, A.J. (1995) Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils. J. Biol. Chem. 270, 16542-16548.
  • Drożdż, R., Naskalski, J.W. & Sznajd, J. (1988) Oxidation of amino-acids in reaction with myeloperoxidase chloride and hydrogen peroxide. Biochim. Biophys. Acta 957, 47-52.
  • Heinecke, J.W. (1999) Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders. J. Lab. Clin. Med. 133, 321-325.
  • Kettle, A.J. (1996) Neutrophils convert tyrosyl residues in albumin to chlorotyrosine. FEBS Lett. 379, 103-106.
  • Marcinkiewicz, J., Chain, M.B., Olszowska, E., Olszowski, S. & Zgliczyński, J.M. (1991) Enhancement of immunologic properties of ovoalbumin as a result of its chlorination. Int. J. Biochem. 23, 1393-1395.
  • Marcinkiewicz, J., Olszowska, E., Olszowski, S. & Zgliczyński, J.M. (1992) Enhancement of trinitrophenyl-specific humoral response to TNP proteins as the result of carrier chlorination. Immunology 76, 385-388.
  • Naskalski, J.W. (1977) Myeloperoxidase inactivation in the course of catalysis of chlorination of taurine. Biochim. Biophys. Acta 485, 291-300.
  • Norman, F.P. (1967) Preparation of inhibitors of oxitocin. Acetylation of amino and hydroxyl tyrosine groups. J. Biol Chem. 242, 1669-1678.
  • Pereira, W.E., Hoyano, Y., Sumons, R.E., Bacon, V.A. & Dunfield, A.M. (1973) Chlorination studies II. The reaction of aqueous hypochlorous acid with alpha amino acids and dipeptides. Biochem. Biophys. Acta 313, 170-180.
  • Thomas, E.L., Grisham, M.B. & Jefferson, M.M. (1986) Preparation and characterization of chloramines. Methods Enzymol. 132, 569-585.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv48i1p271kz
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.