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Báo cáo Y học: Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes
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Arecombinant streptococcalC5apeptidasewas expressed in Escherichia coliand its catalytic properties and thermal sta-bility were subjected to examination. It was shown that the NH2 -terminal region ofC5a peptidase (Asn32–Asp79/ Lys90) forms the pro-sequence segment. Upon maturation the propeptide is hydrolyzed either via an autocatalytic intramolecular cleavage or by exogenous protease strepto-pain. At pH 7.4 the enzyme exhibited maximum activity in the narrow range oftemperatures between 40 and 43C....
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