| Stability profiles of nepenthesin in urea and guanidine hydrochloride: comparison with porcine pepsin A. | |
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MedLine Citation:
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PMID: 21071863 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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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Authors:
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Keiko Kubota; Yuya Metoki; Senarath B P Athauda; Chiaki Shibata; Kenji Takahashi |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't Date: 2010-11-07 |
Journal Detail:
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Title: Bioscience, biotechnology, and biochemistry Volume: 74 ISSN: 1347-6947 ISO Abbreviation: Biosci. Biotechnol. Biochem. Publication Date: 2010 |
Date Detail:
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Created Date: 2010-11-30 Completed Date: 2011-03-23 Revised Date: 2011-08-11 |
Medline Journal Info:
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Nlm Unique ID: 9205717 Medline TA: Biosci Biotechnol Biochem Country: Japan |
Other Details:
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Languages: eng Pagination: 2323-6 Citation Subset: IM |
Affiliation:
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Laboratory of Molecular Biochemistry, School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Aspartic Acid Endopeptidases / chemistry* Enzyme Stability* / drug effects Guanidine / pharmacology Hydrogen-Ion Concentration Pepsin A / chemistry* Plant Proteins Protein Denaturation / drug effects Sarraceniaceae / enzymology* Swine Temperature Urea / pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Plant Proteins; 113-00-8/Guanidine; 57-13-6/Urea; EC 3.4.23.-/Aspartic Acid Endopeptidases; EC 3.4.23.1/Pepsin A |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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