Print Email Facebook Twitter Conformational stability of the potato serine protease inhibitor group 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 AggregationEquilibriumPSPIDisulfideTetramerConformationControlled studyDifferential scanning calorimetryFluorescence spectroscopyKineticsNonhumanPotatoThermodynamicsUltraviolet spectroscopyCalorimetry, Differential ScanningCircular DichroismDrug StabilityGuanidineHeatProtein ConformationSerine Proteinase InhibitorsSolanum tuberosumSpectrometry, FluorescenceSolanum tuberosum To reference this document use: http://resolver.tudelft.nl/uuid:3829741e-81a3-4092-852a-013496f05653 TNO identifier 238439 ISSN 0021-8561 Source Journal of Agricultural and Food Chemistry, 53 (8), 3191-3196 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.