Article

Stability profiles of nepenthesin in urea and guanidine hydrochloride: comparison with porcine pepsin A.

Laboratory of Molecular Biochemistry, School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan.
Bioscience Biotechnology and Biochemistry (impact factor: 1.28). 11/2010; 74(11):2323-6. pp.2323-6
Source: PubMed

ABSTRACT Nepenthesin, an aspartic endopeptidase from the pitcher fluid of Nepenthes, was found to be markedly less stable than porcine pepsin A when treated with urea or guanidine hydrochloride. This is in sharp contrast with its remarkably high pH/temperature stability as compared with porcine pepsin A. No protein with such a stability profile has been reported to date.

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Keywords

aspartic endopeptidase
 
guanidine hydrochloride
 
markedly less stable
 
porcine pepsin
 
porcine pepsin A
 

Keiko Kubota