Searched for: subject%3A%22Protein%255C%2BStructure%252C%255C%2BQuaternary%22
(1 - 8 of 8)
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van Boxtel, E.L. (author), van den Broek, L.A.M. (author), Koppelman, S.J. (author), Gruppen, H. (author), TNO Kwaliteit van Leven (author)
Legumin proteins Ara h 3 from peanuts and glycinin from soybeans are increasingly described as important allergens. The stability of an allergen's IgE binding capacity towards heating and digestion is considered an important characteristic for food allergens. We investigated the effects of heating and digestion on the IgE binding of Ara h 3 and...
article 2008
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van Boxtel, E.L. (author), van Beers, M.M.C. (author), Koppelman, S.J. (author), van den Broek, L.A.M. (author), Gruppen, H. (author), TNO Kwaliteit van Leven (author)
Ara h 1, a major peanut allergen, is known as a stable trimeric protein. Nevertheless, upon purification of native Ara h 1 from peanuts using only size exclusion chromatography, the allergen appeared to exist in an oligomeric structure, rather than as a trimeric structure. The oligomeric structure was independent of the salt concentration...
article 2006
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Broersen, K. (author), Voragen, A.G.J. (author), Hamer, R.J. (author), de Jongh, H.H.J. (author), TNO Voeding (author)
In this article we show how various degrees of glycosylation can be used to control the thermal stability of proteins. The primary amines of β-lactoglobulin were glycosylated with glucose or fructose within a range of non-denaturing reaction parameters. The modified fractions were characterized and analyzed for structural stability and...
article 2004
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Kosters, H.A. (author), Broersen, K. (author), de Groot, J. (author), Simons, J.W.F.A. (author), Wierenga, P. (author), de Jongh, H.H.J. (author), TNO Voeding (author)
Processing of ovalbumin may result in proteins that differ more than 23°C in denaturation temperature while the structural fold is not significantly affected. This is achieved by 1) conversion of positive residues into negative ones (succinylation); 2) elimination of negative charges (methylation); 3) reducing the proteins hydrophobic exposure ...
article 2003
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TNO Voeding (author), Pouvreau, L. (author), Gruppen, H. (author), van Koningsveld, G.A. (author), van den Broek, L.A.M. (author), Voragen, A.G.J. (author)
The gene of the most abundant protease inhibitor in potato cv. Elkana was isolated and sequenced. The deduced amino acid sequence of this gene showed 98% identity with potato serine protease inhibitor (PSPI), a member of the Kunitz family. Therefore, the most abundant protease inhibitor was considered to be one of the isoforms of PSPI. The PSPI...
article 2003
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Smit, E. (author), Oling, F. (author), Demel, R. (author), Martinez, B. (author), Pouwels, P.H. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
Lactobacillus acidophilus, like many other bacteria, harbors a surface layer consisting of a protein (SA-protein) of 43 kDa. SA-protein could be readily extracted and crystallized in vitro into large crystalline patches on lipid monolayers with a net negative charge but not on lipids with a net neutral charge. Reconstruction of the S-layer from...
article 2001
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Sandbæk, G. (author), Bjørnsen, S. (author), Sobel, J.H. (author), Nieuwenhuizen, W. (author), Matsueda, G. (author), Brosstad, F. (author), Gaubius Instituut TNO (author)
The aim of this study was to characterize soluble fibrin(ogen) species in human, arterial, in-vivo-formed thrombi, using the immunoblotting technique. Specimens were collected via intra-arterial catheters in six patients scheduled for catheter-directed thrombolysis. Unreduced and reduced samples of the supernatants from the arterial thrombi...
article 2000
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TNO Voeding (author), Lakemond, C.M.M. (author), de Jongh, H.H.J. (author), Hessing, M. (author), Gruppen, H. (author), Voragen, A.G.J. (author)
This study describes the relationship between the solubility of glycinin, a major soy protein, and its structural properties at a quaternary, tertiary, and secondary folding level under conditions representative for food products. When the ionic strength is lowered from 0.5 to 0.2 or 0.03, the basic polypeptides shift more to the exterior of the...
article 2000
Searched for: subject%3A%22Protein%255C%2BStructure%252C%255C%2BQuaternary%22
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