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Requirement of intact human ceruloplasmin for the glutathione‐linked peroxidase activity
Author(s) -
Kim In Gyu,
Park Seon Young
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01253-8
Subject(s) - ceruloplasmin , chemistry , glutathione , proteolysis , gpx6 , peroxidase , biochemistry , glutathione peroxidase , glutathione reductase , gpx3 , enzyme
Structural integrity may be needed for the glutathione‐linked peroxidase activity of human ceruloplasmin. Intact human ceruloplasmin has a potent peroxidase property to decompose H 2 O 2 in the presence of reduced glutathione. However, the fragment of approximately 116 000 Da produced by proteolytic degradation had less than one‐third of the glutathione‐linked peroxidase activity of intact ceruloplasmin. When further proteolysis occurred, glutathione‐linked peroxidase activity of human ceruloplasmin disappeared. In contrast, ceruloplasmin (116 000 Da and <96 000 Da) fragmented by proteolysis significantly removed H 2 O 2 irrespective of the presence of reduced glutathione. Although proteolytic fragmentation of ceruloplasmin occurs, the antioxidant activity of ceruloplasmin that prevents DNA strand breaks in a metal‐catalyzed reaction system was significantly maintained.