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Biochim Biophys Acta. 1988 Aug 31;956(1):58-62.

A pulse radiolysis investigation of the reactions of myeloperoxidase with superoxide and hydrogen peroxide.

Author information

1
Department of Pathology, Christchurch School of Medicine, Christchurch Hospital, New Zealand.

Abstract

Using pulse radiolysis, the rate constant for the reaction of ferric myeloperoxidase with O2- to give compound III was measured at pH 7.8, and values of 2.1.10(6) M-1.s-1 for equine ferric myeloperoxidase and 1.1.10(6) M-1.s-1 for human ferric myeloperoxidase were obtained. Under the same conditions, the rate constant for the reaction of human ferric myeloperoxidase with H2O2 to give compound I was 3.1.10(7) M-1.s-1. Our results indicate that although the reaction of ferric myeloperoxidase with O2- is an order of magnitude slower than with H2O2, the former reaction is sufficiently rapid to influence myeloperoxidase-dependent production of hypochlorous acid by stimulated neutrophils.

PMID:
2841980
DOI:
10.1016/0167-4838(88)90297-x
[Indexed for MEDLINE]

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