The reductive cleavage of myeloperoxidase in half, producing enzymically active hemi-myeloperoxidase.

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The reductive cleavage of myeloperoxidase in half, producing enzymically active hemi-myeloperoxidase.

Reduction and alkylation of human myeloperoxidase under nondenaturing conditions results in the cleavage of this enzyme. Sedimentation equilibrium data is presented which shows that the molecular weight of the cleavage product (78,000 +/- 2,000) is half that of the native enzyme (153,000 +/- 4,000). We conclude that the cleavage product is the half-enzyme hemi-myeloperoxidase. Hemi-myeloperoxid...

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The changes in the oxidation state of the leucocyte enzyme myeloperoxidase, induced by buffer and thiols, were studied with visible-light-absorption spectroscopy. It was concluded that phosphate buffer contains small amounts of H2O2 and that thiols, when added to buffer, induce the generation of minute amounts of superoxide radical anion. These minute amounts of reduced oxygen species are sugge...

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Biological Variation of Myeloperoxidase

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The prosthetic group of myeloperoxidase.

In general, when hemoproteins are treated with acidified acetone, the protein is precipitated, while the heme remains in solution. Exceptions are cytochrome c, lactoperoxidase, and myeloperoxidase; the linkages between heme and protein in these instances being covalent. While the nature of the linkages in cytochrome c and lactoperoxidase have been characterized, that present in myeloperoxidase ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1981

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)69420-2