منابع مشابه
Superoxide anions mediate veratridine-induced cytochrome c release and caspase activity in bovine chromaffin cells.
1. Mitochondrial mechanisms involved in veratridine-induced chromaffin cell death have been explored. 2. Exposure to veratridine (30 micro M, 1 h) produces cytochrome c release to the cytoplasm that seems to be mediated by superoxide anions and that is blocked by cyclosporin A (10 micro M), MnTBAP (10 nM), catalase (100 IU ml(-1)) and vitamin E (50 micro M). 3. Following veratridine treatment, ...
متن کاملDetection of the superoxide radical anion using various alkanethiol monolayers and immobilized cytochrome c.
The superoxide radical anion (SO) is a critical biomarker for monitoring cellular stress responses. Electrochemical SO biosensors are frequently constructed through the covalent immobilization of cytochrome c (Cyt c) onto self-assembled monolayers (SAMs); however, a detailed comparison of these systems as well as configuration influence on SO detection is needed to enable robust applications. T...
متن کاملNADPH oxidase of neutrophils forms superoxide anion but does not reduce cytochrome c and dichlorophenolindophenol.
Superoxide (O-2) production by partially purified NADPH oxidase from guinea pig neutrophils was markedly increased when the cells were activated by exposure to phorbol-myristate acetate. On the contrary, NADPH-dependent cytochrome c and 2,6-dichlorophenolindophenol (DCIP) reductase activities in preparations from resting and activated neutrophils were similar. The apparent Km values for NADH an...
متن کاملCytochrome c
How is it made? Cytochrome c is synthesized from two inactive precursor molecules: apocytochrome c (a protein that is encoded by a nuclear gene and imported into mitochondria) and heme (which is synthesized in mitochondria). The covalent attachment of apocytochrome c to heme is catalyzed by heme lyase and creates cytochrome c, a 14.5 kDa protein that is normally confined to the intermembrane sp...
متن کاملSuperoxide dismutase-inhibitible reduction of cytochrome c by the alloxan radical. Implications for alloxan cytotoxicity.
Cytochrome c was reduced when superoxide was generated from xanthine oxidase in the presence of alloxan, and by the reaction of alloxan and with reduced glutathione. In each case, most of the reduction was inhibited by superoxide dismutase, but considerably more enzyme was required than with superoxide alone. This indicates that the superoxide dismutase-inhibitible cytochrome c reduction was ma...
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ژورنال
عنوان ژورنال: JBIC Journal of Biological Inorganic Chemistry
سال: 2013
ISSN: 0949-8257,1432-1327
DOI: 10.1007/s00775-013-1020-6