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A chemical modification of myeloperoxidase and lactoperoxidase with 2‐(O‐methoxypolyethylene glycol)‐4,6‐dichloro‐s‐triazine (activated PEG 1 )
Author(s) -
Odajima Takeshi,
Onishi Mihoko
Publication year - 1998
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/(sici)1099-0844(199806)16:2<123::aid-cbf777>3.0.co;2-4
Subject(s) - chemistry , lactoperoxidase , hydrogen peroxide , myeloperoxidase , ferric , nuclear chemistry , polyethylene glycol , peroxidase , bromide , medicinal chemistry , enzyme , inorganic chemistry , organic chemistry , medicine , inflammation
The modification of myeloperoxidase and lactoperoxidase with 2‐(O‐methoxypolethylene glycol)‐4, 6‐dichloro‐s‐triazine, an activated polyethylene glycol (PEG 1 ), was investigated. The modification caused a shift of the Soret band in the light absorption spectrum, from 430 nm to 418 nm in the case of myeloperoxidase (native ferric form), and from 412 nm to 406 nm in the case of lactoperoxidase (native ferric form). PEG 1 ‐modified myeloperoxidase and PEG 1 ‐modified lactoperoxidase both failed to bind with antiserum to the respective native enzyme, but both retained respectively 4·5±0·3 per cent (mean±SE, n =5) and 0·6±0·2 per cent (mean±SE, n =5) of the activities of peroxidation of the hydrogen donor o ‐methoxyphenol in comparison with the native enzyme, and 1·5±0·2 per cent (mean±SE, n =5) and 1·2±0·2 per cent (mean±SE, n =5) of the activities of destruction of fuchsin basic in the presence of hydrogen peroxide and a halide, bromide. The pH dependencies of the peroxidating activities were almost the same as those of the corresponding native enzymes, but both the optimal pHs of the reactions involving the destruction of fuchsin basic were shifted by approximately 1·0 pH unit toward neutral pH compared with the respective native enzymes. © 1998 John Wiley & Sons, Ltd.