Oxidative folding of hirudin in human serum
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چکیده
منابع مشابه
Oxidative folding of hirudin in human serum.
Human serum contains factors that promote oxidative folding of disulphide proteins. We demonstrate this here using hirudin as a model. Hirudin is a leech-derived thrombin-specific inhibitor containing 65 amino acids and three disulphide bonds. Oxidative folding of hirudin in human serum is shown to involve an initial phase of rapid disulphide formation (oxidation) to form the scrambled isomers ...
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The folding of hirudin undergoes an initial stage of non-specific packing, followed by consolidation (re-organization) of partially packed intermediates to attain the native structure [Chatrenet and Chang (1993) J. Biol. Chem. 268, 20988-20996]. Non-specific packing leads to the formation of scrambled hirudins as folding intermediates. A systematic study was carried out to search for conditions...
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The folding pathway of hirudin was analyzed by structural characterization and stop/go folding experiments of acid-trapped intermediates. The results show that the folding is initiated by a near-random packing, followed by the reorganization and fine adjustment of partially compact intermediates to attain the active molecule. The process of packing is observed as the unfolded hirudin flows sequ...
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The endoplasmic reticulum (ER) provides an environment that is highly optimized for oxidative protein folding. Rather than relying on small molecule oxidants like glutathione, it is now clear that disulfide formation is driven by a protein relay involving Ero1, a novel conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular oxygen and in turn acts as...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2006
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20051660