Title : Balancing conformational and oxidative kinetic traps during the folding of bovine pancreatic trypsin inhibitor (BPTI) with glutathione and glutathione disulfide.

Pub. Date : 2008 Jan 23

PMID : 18166059






4 Functional Relationships(s)
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1 Balancing conformational and oxidative kinetic traps during the folding of bovine pancreatic trypsin inhibitor (BPTI) with glutathione and glutathione disulfide. Glutathione Disulfide spleen trypsin inhibitor I Bos taurus
2 Under traditional conditions, 0.125 mM glutathione disulfide (GSSG) and no glutathione (GSH), the folding pathway of BPTI proceeds through a nonproductive route via N* (a two disulfide intermediate), or a productive route via N" (and other two disulfide intermediates which are in rapid equilibrium with N"). Glutathione Disulfide spleen trypsin inhibitor I Bos taurus
3 Under traditional conditions, 0.125 mM glutathione disulfide (GSSG) and no glutathione (GSH), the folding pathway of BPTI proceeds through a nonproductive route via N* (a two disulfide intermediate), or a productive route via N" (and other two disulfide intermediates which are in rapid equilibrium with N"). Glutathione Disulfide spleen trypsin inhibitor I Bos taurus
4 Interestingly, BPTI folds more efficiently in the presence of 5 mM GSSG and 5 mM GSH than it does under traditional conditions. Glutathione Disulfide spleen trypsin inhibitor I Bos taurus