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 protein with such a stability profile has been reported to date.
Laboratory of Molecular Biochemistry, School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan.
Keiko
K
Kubota
Yuya
Y
Metoki
Senarath B P
SB
Athauda
Chiaki
C
Shibata
Kenji
K
Takahashi
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D004795:Enzyme Stability / Q000187:drug effects; D019791:Guanidine / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D010434:Pepsin A / Q000737:chemistry*; D010940:Plant Proteins; D011489:Protein Denaturation / Q000187:drug effects; D052583:Sarraceniaceae / Q000201:enzymology*; D013552:Swine; D013696:Temperature; D014508:Urea / Q000494:pharmacology
D010940:Plant Proteins; D014508:Urea; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A; D019791:Guanidine