Investigation of the redox state of recombinant horseradish peroxidase produced in inclusion bodies and factors affecting the efficiency of refolding.
White
C
C
Biochemistry Department, School of Biological Sciences, University of Sussex.
Sampson
C
C
Burke
J
J
Smith
A
A
D003001:Cloning, Molecular; D004229:Dithiothreitol / Q000494:pharmacology; D004926:Escherichia coli; D005813:Genes, Synthetic; D005978:Glutathione / Q000031:analogs & derivatives / Q000494:pharmacology; D019803:Glutathione Disulfide; D006735:Horseradish Peroxidase / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D011489:Protein Denaturation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism
D011994:Recombinant Proteins; D006735:Horseradish Peroxidase; D005978:Glutathione; D004229:Dithiothreitol; D019803:Glutathione Disulfide