Stability Profiles of Nepenthesin in Urea and Guanidine Hydrochloride: Comparison with Porcine Pepsin A

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...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2010, Vol.74 (11), p.2323-2326
Main Authors: KUBOTA, Keiko, METOKI, Yuya, ATHAUDA, Senarath B. P., SHIBATA, Chiaki, TAKAHASHI, Kenji
Format: Article
Language:English
Subjects:
Animals
Aspartic Acid Endopeptidases - chemistry
Biological and medical sciences
denaturation
Enzyme Stability - drug effects
Fundamental and applied biological sciences. Psychology
Guanidine - pharmacology
guanidine hydrochloride
Hydrogen-Ion Concentration
Nepenthes
nepenthesin
Pepsin A - chemistry
Plant Proteins
porcine pepsin A
Protein Denaturation - drug effects
Sarraceniaceae - enzymology
Swine
Temperature
urea
Urea - pharmacology
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Summary: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.
ISSN:0916-8451
1347-6947
1347-6947
DOI:10.1271/bbb.100391