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Superoxide dismutase activity of a novel macromolecular manganese porphyrin
Author(s) -
Kawakami H.,
Ohse T.,
Kawano M.,
Nagaoka S.
Publication year - 1999
Publication title -
polymers for advanced technologies
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.61
H-Index - 90
eISSN - 1099-1581
pISSN - 1042-7147
DOI - 10.1002/(sici)1099-1581(199905)10:5<270::aid-pat873>3.0.co;2-c
Subject(s) - sma* , superoxide dismutase , porphyrin , maleic anhydride , manganese , chemistry , nuclear chemistry , biochemistry , biophysics , antioxidant , organic chemistry , polymer , copolymer , biology , mathematics , combinatorics
The discovery of a novel superoxide dismutase (SOD) mimic which demonstrates SOD activity, chemical stability in H 2 O 2 solution and long half‐life in circulation is reported. The SOD mimic consists of a manganese porphyrin (MnP) with SOD activity and a polymer (poly (styrene‐co‐maleic anhydride); SMA) with biological characteristics. The SOD activity of SMA‐MnP at pH = 8.1 measured using the stopped‐flow kinetic analysis technique to monitor the decay of superoxide directly was 1.1 (± 0.1) × 10 6 M‐1 sec‐1. It is postulated that the reduction by O 2 ·− of the oxidized SMA‐Mn(III) is slow, while the oxidation of the reduced SMA‐Mn(II) by O 2 ·− is very fast. The retention times of SMA‐MnP in the circulation of rabbits were determined. In vivo , SMA‐MnP that binds to the warfarin site on albumin showed an enhanced half‐life in the circulation. Additionally, in vitro SMA‐MnP indicated an excellent stability to H 2 O 2 . Copyright © 1999 John Wiley & Sons, Ltd.