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

Keiko Kubota | Zendy; Yuya METOKI | Zendy; Senarath B. P. Athauda | Zendy; Chiaki Shibata | Zendy; Kenji Takahashi | Zendy

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

Author(s) -

Keiko Kubota,

Yuya METOKI,

Senarath B. P. Athauda,

Chiaki Shibata,

Kenji Takahashi

Publication year - 2010

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.100391

Subject(s) - guanidine , pepsin , urea , hydrochloride , chemistry , chromatography , biochemistry , enzyme

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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