Abstract
Bacillus subtilis pyrrolidone carboxyl peptidase (Pep) overexpressed in Escherichia coli was purified to homogeneity in less than 12 h using ammonium sulphate precipitation and hydrophobic interaction chromatography. The enzyme, which removes amino-terminal l-pyroglutamic acid from peptides, appears to be a tetramer of 25 200 molecular mass subunits. The protein cross-reacted with polyclonal antibodies raised against Pep from Streptococcus pyogenes. The overexpressed enzyme exhibits an absolute substrate specificity towards N-terminal pyroglutamyl residues with a Michaelis constant of 1.04 m M for l-pyroglutamyl-β-naphthylamide. The enzyme could be used for the removal of pyroglutamyl residues that block amino termini of proteins and peptides before performing Edman sequential degradation.
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Schedule a callMore From: Journal of Chromatography B: Biomedical Sciences and Applications
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