| Literature DB >> 15264937 |
Lambertus A M van den Broek1, Laurice Pouvreau, Gijs Lommerse, Bert Schipper, Gerrit A Van Koningsveld, Harry Gruppen.
Abstract
In the present study the structural properties of potato protease inhibitor 1 (PI-1) were studied as a function of temperature to elucidate its precipitation mechanism upon heating. A cDNA coding for PI-1 from cv. Bintje was cloned and expressed in Pichia pastoris. Using the recombinant PI-1 it was suggested that PI-1 behaves as a hexameric protein rather than as a pentamer, as previously proposed in the literature. The recombinant protein seems either to have a predominantly unordered structure or to belong to the beta-II proteins. Differential scanning calorimetry analysis of PI-1 revealed that its thermal unfolding occurs via one endothermic transition in which the hexameric PI-1 probably unfolds, having a dimer instead of a monomer as cooperative unit. The transition temperature for the recombinant PI-1 was 88 degrees C. Similar results were obtained for a partially purified pool of native PI-1 from cv. Bintje. Copyright 2004 American Chemical SocietyEntities:
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Year: 2004 PMID： 15264937 DOI： 10.1021/jf049832x
Source DB: PubMed Journal: J Agric Food Chem ISSN： 0021-8561 Impact factor: 5.279