Comparative study of mature and zymogen mite cysteine protease stability and pH unfolding.


Abstract

Papain-like proteases (CA1) are synthesized as inactive precursors carrying an N-terminal propeptide, which is further removed under acidic conditions to generate active enzymes. Study holds ProTherm entries: 25848, 25849, 25850, 25851, 25852 Extra Details: mature protease pH-induced unfolding; Propeptide; Der p 1; Cysteine protease; Stability; Mechanism of activation; Fluorescence quenching; Thermal denaturation; Allergen; Zymogen

Submission Details

ID: QbWe9iY

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:56 p.m.

Version: 1

Publication Details
Chevigné A;Dumez ME;Dumoulin M;Matagne A;Jacquet A;Galleni M,Biochim. Biophys. Acta (2010) Comparative study of mature and zymogen mite cysteine protease stability and pH unfolding. PMID:20682463
Additional Information

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