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

Keiko KUBOTA; Yuya METOKI; Senarath B. P. ATHAUDA; Chiaki SHIBATA; Kenji TAKAHASHI

doi:10.1271/bbb.100391

This article has now been updated. Please use the final version.

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

Keiko KUBOTA, Yuya METOKI, Senarath B. P. ATHAUDA, Chiaki SHIBATA, Kenji TAKAHASHI

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Keywords: denaturation, guanidine hydrochloride, nepenthesin, porcine pepsin A, urea

JOURNAL FREE ACCESS Advance online publication

Article ID: 100391

DOI https://doi.org/10.1271/bbb.100391

The final version of this article is now available: Vol. 74 (2010) , No. 11 p.2323

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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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