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1 Effect of heat-induced aggregation on the IgE binding of patatin (Sol t 1) is dominated by other potato proteins
article 2002    
Author: Koppelman, S.J. · Koningsveld, G.A. van · Knulst, A.C. · Gruppen, H. · Pigmans, I.G.A.J. · Jongh, H.H.J. de
Keywords: Nutrition · Adult · Allergens · Calorimetry, Differential Scanning · Carboxylic Ester Hydrolases · Circular Dichroism · Food Hypersensitivity · Heat · Humans · Immunoglobulin E · Plant Proteins · Protein Denaturation · Protein Folding · Solanum tuberosum · Spectrometry, Fluorescence · Tryptophan
[Abstract]

2 The presence of heat-stable conformers of ovalbumin affects properties of thermally formed aggregates
article 2003    
Author: Groot, J.de · Jongh, H.H.J.de
Keywords: Nutrition · Food technology · Aggregation · Ovalbumin · Protein denaturation · Stokes radius · Turbidity · ovalbumin · article · chemical reaction kinetics · heat treatment · pH · priority journal · protein aggregation · protein analysis · protein denaturation · protein stability · thermostability · turbidity · Animals · Calorimetry, Differential Scanning · Chickens · Heat · Kinetics · Ovalbumin · Protein Conformation · Time Factors · Gallus gallus
[Abstract]

3 Identification of pitfalls in the analysis of heat capacity changes of β-lactoglobulin A
article 2005    
Author: Teeffelen, A.M.M. van · Meinders, M.B.J. · Jongh, H.H.J. de
Keywords: Nutrition · Food technology · Calorimetry · Heat capacity · Protein · Spectroscopy · Thermodynamics · beta lactoglobulin · tryptophan · article · circular dichroism · data analysis · differential scanning calorimetry · fluorescence · protein conformation · protein denaturation · protein folding · sensitivity analysis · thermal analysis · ultraviolet radiation · validation process · Animals · Calorimetry · Calorimetry, Differential Scanning · Cattle · Circular Dichroism · Heat · Lactoglobulins · Milk · Protein Denaturation · Protein Folding · Sensitivity and Specificity · Spectrometry, Fluorescence · Temperature · Thermodynamics · Tryptophan · Ultraviolet Rays · Urea
[Abstract]

4 Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties
article 1999    
Author: Koppelman, S.J. · Bruijnzeel-Koomen, C.A.F.M. · Hessing, M. · Jongh, H.H.J. de
Keywords: Allergen · Allergenicity · Animal cell · Conformational transition · Heat tolerance · Isoelectric point · Nonhuman · Peanut · Priority journal · Protein denaturation · Protein family · Protein folding · Protein secondary structure · Solubility · Thermostability · Adult · Allergens · Arachis hypogaea · Calorimetry, Differential Scanning · Chromatography, Gel · Circular Dichroism · Glycoproteins · Heat · Humans · Immunoglobulin E · Plant Proteins · Protein Conformation · Spectrophotometry, Ultraviolet · Animalia · Ara · Arachis hypogaea
[PDF] [Abstract]

5 Heat-induced conformational changes of patatin, the major potato tuber protein
article 1998    
Author: Pots, A.M. · Jongh, H.H.J. de · Gruppen, H. · Hamer, R.J. · Voragen, A.G.J.
Keywords: Nutrition · Conformational change · Patatin · Solanum tuberosum · Enzyme · Vegetable protein · Alpha helix · Circular dichroism · Conformational transition · Differential scanning calorimetry · Enzyme conformation · Enzyme inactivation · Fluorescence spectroscopy · Infrared spectroscopy · Nonhuman · Potato · Priority journal · Protein denaturation · Protein folding · Protein secondary structure · Temperature · Thermostability · Butyrates · Calorimetry, Differential Scanning · Carboxylic Ester Hydrolases · Circular Dichroism · Enzyme Stability · Esterases · Plant Proteins · Protein Conformation · Protein Folding · Protein Structure, Secondary · Protein Structure, Tertiary · Solanum tuberosum · Spectrometry, Fluorescence · Spectroscopy, Fourier Transform Infrared · Temperature · Tryptophan · Solanum tuberosum · Tuberosum
[Abstract]

6 Characterization of Pea Vicilin. 1. Denoting Convicilin as the α-Subunit of the Pisum Vicilin Family
article 2004    
Author: O'Kane, F.E. · Happe, R.P. · Vereijken, J.M. · Gruppen, H. · Boekel, M.A.J.S. van
Keywords: Nutrition · Food technology · Convicillin · Heterogeneity · Pisum · Purification · Storage proteins · Subunit composition · Vicilin · Convicilin · Globulin · Oligomer · Polypeptide · Unclassified drug · Vegetable protein · Vicilin · Vicilin 1 · Vicilin 2 · Acidity · Alkalinity · Alpha chain · Circular dichroism · Differential scanning calorimetry · Extraction · Flour · Fractionation · Multigene family · Nonhuman · Pea · PH · Polyacrylamide gel electrophoresis · Protein analysis · Protein family · Protein purification · Separation technique · Solubility · Calorimetry, Differential Scanning · Chemical Fractionation · Electrophoresis, Polyacrylamide Gel · Hydrogen-Ion Concentration · Peas · Plant Proteins · Protein Structure, Secondary · Solubility · Pisum · Pisum sativum
[Abstract]

7 Peanut allergen Ara h 3: Isolation from peanuts and biochemical characterization
article 2003    
Author: Koppelman, S.J. · Knol, E.F. · Vlooswijk, R.A.A. · Wensing, M. · Knulst, A.C. · Hefle, S.L. · Gruppen, H. · Piersma, S.
Keywords: Nutrition Health · Food technology · Allergens · IgE-binding · Peanut · Purification · allergen · Ara h 3 antigen · complementary DNA · glycinin · immunoglobulin E · peanut antigen · protein subunit · unclassified drug · allergenicity · amino acid sequence · amino terminal sequence · antigen binding · article · biochemistry · enzyme linked immunosorbent assay · gel permeation chromatography · nonhuman · peanut · peanut allergy · priority journal · protein analysis · protein folding · protein isolation · protein processing · protein purification · protein structure · protein unfolding · Western blotting · Allergens · Amino Acid Sequence · Arachis hypogaea · Calorimetry, Differential Scanning · Chromatography, Ion Exchange · Electrophoresis, Polyacrylamide Gel · Enzyme-Linked Immunosorbent Assay · Humans · Immunoblotting · Immunoglobulin E · Peanut Hypersensitivity
[Abstract]

Search results also available in MS Excel format.

Showing 1 to 7 of 7 found. | Sort by date