Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation

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Hypochlorite-induced damage to proteins : formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. / Hawkins, C L; Davies, Michael Jonathan.

In: Biochemical Journal, Vol. 332 ( Pt 3), 15.06.1998, p. 617-25.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Hawkins, CL & Davies, MJ 1998, 'Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation', Biochemical Journal, vol. 332 ( Pt 3), pp. 617-25.

APA

Hawkins, C. L., & Davies, M. J. (1998). Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. Biochemical Journal, 332 ( Pt 3), 617-25.

Vancouver

Hawkins CL, Davies MJ. Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. Biochemical Journal. 1998 Jun 15;332 ( Pt 3):617-25.

Author

Hawkins, C L ; Davies, Michael Jonathan. / Hypochlorite-induced damage to proteins : formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. In: Biochemical Journal. 1998 ; Vol. 332 ( Pt 3). pp. 617-25.

Bibtex

@article{a80ea30ed5e04208881ca0a691571ac6,
title = "Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation",
abstract = "Stimulated monocytes and neutrophils generate hypochlorite (HOCl) via the release of the enzyme myeloperoxidase and hydrogen peroxide. HOCl damages proteins by reaction with amino acid side-chains or backbone cleavage. Little information is available about the mechanisms and intermediates involved in these reactions. EPR spin trapping has been employed to identify radicals on proteins, peptides and amino acids after treatment with HOCl. Reaction with HOCl gives both high- and low-molecular-mass nitrogen-centred, protein-derived radicals; the yield of the latter increases with both higher HOCl:protein ratios and enzymic digestion. These radicals, which arise from lysine side-chain amino groups, react with ascorbate, glutathione and Trolox. Reaction of HOCl-treated proteins with excess methionine eliminates radical formation, which is consistent with lysine-derived chloramines (via homolysis of N-Cl bonds) being the radical source. Incubation of HOCl-treated proteins, after removal of excess oxidant, gives rise to both nitrogen-centred radicals, over a period of hours, and time-dependent fragmentation of the protein. Treatment with excess methionine or antioxidants (Trolox, ascorbate, glutathione) protects against fragmentation; urate and bilirubin do not. Chloramine formation and nitrogen-centred radicals are therefore key species in HOCl-induced protein fragmentation.",
keywords = "Amino Acids, Animals, Antioxidants, Cattle, Chloramines, Electron Spin Resonance Spectroscopy, Electrophoresis, Polyacrylamide Gel, Free Radicals, Humans, Hypochlorous Acid, Lysine, Oligopeptides, Proteins, Serum Albumin, Spin Trapping, Time Factors",
author = "Hawkins, {C L} and Davies, {Michael Jonathan}",
year = "1998",
month = "6",
day = "15",
language = "English",
volume = "332 ( Pt 3)",
pages = "617--25",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",

}

RIS

TY - JOUR

T1 - Hypochlorite-induced damage to proteins

T2 - formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation

AU - Hawkins, C L

AU - Davies, Michael Jonathan

PY - 1998/6/15

Y1 - 1998/6/15

N2 - Stimulated monocytes and neutrophils generate hypochlorite (HOCl) via the release of the enzyme myeloperoxidase and hydrogen peroxide. HOCl damages proteins by reaction with amino acid side-chains or backbone cleavage. Little information is available about the mechanisms and intermediates involved in these reactions. EPR spin trapping has been employed to identify radicals on proteins, peptides and amino acids after treatment with HOCl. Reaction with HOCl gives both high- and low-molecular-mass nitrogen-centred, protein-derived radicals; the yield of the latter increases with both higher HOCl:protein ratios and enzymic digestion. These radicals, which arise from lysine side-chain amino groups, react with ascorbate, glutathione and Trolox. Reaction of HOCl-treated proteins with excess methionine eliminates radical formation, which is consistent with lysine-derived chloramines (via homolysis of N-Cl bonds) being the radical source. Incubation of HOCl-treated proteins, after removal of excess oxidant, gives rise to both nitrogen-centred radicals, over a period of hours, and time-dependent fragmentation of the protein. Treatment with excess methionine or antioxidants (Trolox, ascorbate, glutathione) protects against fragmentation; urate and bilirubin do not. Chloramine formation and nitrogen-centred radicals are therefore key species in HOCl-induced protein fragmentation.

AB - Stimulated monocytes and neutrophils generate hypochlorite (HOCl) via the release of the enzyme myeloperoxidase and hydrogen peroxide. HOCl damages proteins by reaction with amino acid side-chains or backbone cleavage. Little information is available about the mechanisms and intermediates involved in these reactions. EPR spin trapping has been employed to identify radicals on proteins, peptides and amino acids after treatment with HOCl. Reaction with HOCl gives both high- and low-molecular-mass nitrogen-centred, protein-derived radicals; the yield of the latter increases with both higher HOCl:protein ratios and enzymic digestion. These radicals, which arise from lysine side-chain amino groups, react with ascorbate, glutathione and Trolox. Reaction of HOCl-treated proteins with excess methionine eliminates radical formation, which is consistent with lysine-derived chloramines (via homolysis of N-Cl bonds) being the radical source. Incubation of HOCl-treated proteins, after removal of excess oxidant, gives rise to both nitrogen-centred radicals, over a period of hours, and time-dependent fragmentation of the protein. Treatment with excess methionine or antioxidants (Trolox, ascorbate, glutathione) protects against fragmentation; urate and bilirubin do not. Chloramine formation and nitrogen-centred radicals are therefore key species in HOCl-induced protein fragmentation.

KW - Amino Acids

KW - Animals

KW - Antioxidants

KW - Cattle

KW - Chloramines

KW - Electron Spin Resonance Spectroscopy

KW - Electrophoresis, Polyacrylamide Gel

KW - Free Radicals

KW - Humans

KW - Hypochlorous Acid

KW - Lysine

KW - Oligopeptides

KW - Proteins

KW - Serum Albumin

KW - Spin Trapping

KW - Time Factors

M3 - Journal article

C2 - 9620862

VL - 332 ( Pt 3)

SP - 617

EP - 625

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

ER -

ID: 138284414