Article
Achievement of renaturation of subtilisin BPN' by a novel procedure using organic salts and a digestible mutant of Streptomyces subtilisin inhibitor.
FEBS letters - 4 Apr 1994
Matsubara M, Kurimoto E, Kojima S, Miura K, Sakai T
Abstract excerpt
The pro-sequences of proteases have been considered to be required for the refolding of denatured proteases. However, here we report achievement of almost complete restoration of enzymatic activity of subtilisin BPN' in the absence of its pro-sequence. The presence of 2 M potassium acetate in the folding medium enhanced the refolding efficiency of guanidine hydrochloride (GdnHCl)-denatured subtilisin BPN' by up...
Topics
- Acetates
- Acetic Acid
- Amino Acid Sequence
- Bacterial Proteins
- Molecular Sequence Data
- Mutation
- Oligopeptides
- Protein Conformation
- Protein Denaturation
- Streptomyces
- Substrate Specificity