Title of article :
Increased catalytic activity of protein disulfide isomerase using aromatic thiol based redox buffers
Author/Authors :
Jonathan D. Gough، نويسنده , , Watson J. Lees، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2005
Pages :
5
From page :
777
To page :
781
Abstract :
PDI is an enzyme that acts as a chaperone, shufflase, and oxidase during the folding of disulfide-containing proteins. The ability of aromatic thiols to increase the activity of PDI-catalyzed protein folding over that of the standard thiol glutathione (GSH) was measured. 4–Mercaptobenzoic acid (ArSH) increased the activity of PDI by a factor of three.
Keywords :
Protein folding , Aromatic thiols , Thiol–disulfide interchange reaction , RNase A , PDI
Journal title :
Bioorganic & Medicinal Chemistry Letters
Serial Year :
2005
Journal title :
Bioorganic & Medicinal Chemistry Letters
Record number :
795286
Link To Document :
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