Title
Conformational stability of the potato serine protease inhibitor group
Author
Pouvreau, L.
Gruppen, H.
van Koningsveld, G.
van den Broek, L.A.M.
Voragen, A.G.J.
TNO Voeding
Publication year
2005
Abstract
The thermal unfolding of potato serine protease inhibitor (PSPI), the most abundant protease inhibitor group in potato tuber, was measured using far UV CD spectroscopy, fluorescence spectroscopy, and DSC. The results indicate that the thermal as well as the guanidinium-induced unfolding of PSPI occurs via a non-two-state mechanism in which at least one stable intermediate is present. Additionally, the occurrence of aggregation, especially at low scan rates, increases the apparent cooperativity of the unfolding and makes the system kinetically rather than thermodynamically controlled. Aggregate formation seems to occur via a specific mechanism of which PSPI in a tetrameric form is the end product and which may involve disulfide interchanges. © 2005 American Chemical Society. Chemicals / CAS: disulfide, 16734-12-6; guanidine, 113-00-8, 25215-10-5, 50-01-1; Guanidine, 113-00-8; Serine Proteinase Inhibitors
Subject
Aggregation
Equilibrium
PSPI
Disulfide
Tetramer
Conformation
Controlled study
Differential scanning calorimetry
Fluorescence spectroscopy
Kinetics
Nonhuman
Potato
Thermodynamics
Ultraviolet spectroscopy
Calorimetry, Differential Scanning
Circular Dichroism
Drug Stability
Guanidine
Heat
Protein Conformation
Serine Proteinase Inhibitors
Solanum tuberosum
Spectrometry, Fluorescence
Solanum tuberosum
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TNO identifier
238439
ISSN
0021-8561
Source
Journal of Agricultural and Food Chemistry, 53 (8), 3191-3196
Document type
article