Accessing the reproducibility and specificity of pepsin and other aspartic proteases

The aspartic protease pepsin is less specific than other endoproteinases. Because aspartic proteases like pepsin are active at low pH, they are utilized in hydrogen deuterium exchange mass spectrometry (HDX MS) experiments for digestion under hydrogen exchange quench conditions. We investigated the...

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Veröffentlicht in:	Biochimica et biophysica acta 2013-06, Vol.1834 (6), p.1222-1229
Hauptverfasser:	Ahn, Joomi, Cao, Min-Jie, Yu, Ying Qing, Engen, John R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals arginine Arginine - chemistry Arginine - metabolism asparagine Asparagine - chemistry Asparagine - metabolism Aspartic Acid Proteases - chemistry Aspartic Acid Proteases - metabolism Aspergillopepsin deuterium Deuterium - chemistry Deuterium Exchange Measurement digestion Eels Factor XIII Glycine - chemistry Glycine - metabolism Horses Hydrogen - chemistry Hydrogen exchange Mass spectrometry Mass Spectrometry - methods Molecular Sequence Data Monopterus albus Online digestion pepsin Pepsin A - chemistry Pepsin A - metabolism peptides Peptides - chemistry Peptides - metabolism Rabbits Reproducibility of Results Rice field eel Sequence Alignment Sequence Homology, Amino Acid stomach Substrate Specificity Swine
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