Document Detail

Stability profiles of nepenthesin in urea and guanidine hydrochloride: comparison with porcine pepsin A.
MedLine Citation:
PMID:  21071863     Owner:  NLM     Status:  MEDLINE    
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.
Keiko Kubota; Yuya Metoki; Senarath B P Athauda; Chiaki Shibata; Kenji Takahashi
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-11-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  74     ISSN:  1347-6947     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2010  
Date Detail:
Created Date:  2010-11-30     Completed Date:  2011-03-23     Revised Date:  2011-08-11    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  2323-6     Citation Subset:  IM    
Laboratory of Molecular Biochemistry, School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan.
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MeSH Terms
Aspartic Acid Endopeptidases / chemistry*
Enzyme Stability* / drug effects
Guanidine / pharmacology
Hydrogen-Ion Concentration
Pepsin A / chemistry*
Plant Proteins
Protein Denaturation / drug effects
Sarraceniaceae / enzymology*
Urea / pharmacology
Reg. No./Substance:
0/Plant Proteins; 113-00-8/Guanidine; 57-13-6/Urea; EC 3.4.23.-/Aspartic Acid Endopeptidases; EC A

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