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1 Soluble fibrin species in arterial thrombi
article 2000    
Author: Sandbæk, G. · Bjørnsen, S. · Sobel, J.H. · Nieuwenhuizen, W. · Matsueda, G. · Brosstad, F.
Keywords: Aged · Antibodies, Monoclonal · Arteries · Blotting, Western · Female · Fibrin · Fibrinogen · Fibrinopeptide A · Humans · Male · Middle Aged · Molecular Weight · Oxidation-Reduction · Protein Structure, Quaternary · Solubility · Thrombosis
[Abstract]

2 The S-layer protein of Lactobacillus acidophilus ATCC 4356 : identification and characterisation of domains responsible for S-protein assembly and cell wall binding
article 2001    
Author: Smit, E. · Oling, F. · Demel, R. · Martinez, B. · Pouwels, P.H.
Keywords: Biology · Amino Acid Sequence · Bacterial Proteins · Cell Wall · Crystallization · Electrophoresis, Polyacrylamide Gel · Escherichia coli · Lactobacillus acidophilus · Membrane Glycoproteins · Membrane Proteins · Microscopy, Electron · Models, Molecular · Molecular Sequence Data · Peptide Fragments · Phosphatidylserines · Protein Binding · Protein Structure, Quaternary · Protein Structure, Secondary · Protein Structure, Tertiary · Recombinant Fusion Proteins · Sequence Alignment · Sequence Analysis, Protein · Solutions · Trypsin · Escherichia coli · Lactobacillus acidophilus · Lactobacillus casei · Lactobacillus crispatus · Lactobacillus helveticus
[Abstract]

3 Allergen Ara h 1 occurs in peanuts as a large oligomer rather than as a trimer
article 2006    
Author: Boxtel, E.L. van · Beers, M.M.C. van · Koppelman, S.J. · Broek, L.A.M. van den · Gruppen, H.
Keywords: Nutrition · Food technology · Ara h 1 · Food allergen · Peanut · Protein structure · allergen · ammonium sulfate · Ara h 1 protein, Arachis hypogaea · glycoprotein · vegetable protein · article · chemistry · gel chromatography · osmolarity · peanut · plant seed · polyacrylamide gel electrophoresis · precipitation · protein quaternary structure · Allergens · Ammonium Sulfate · Arachis hypogaea · Chromatography, Gel · Electrophoresis, Polyacrylamide Gel · Glycoproteins · Osmolar Concentration · Plant Proteins · Precipitation · Protein Structure, Quaternary · Seeds · Ara · Arachis hypogaea
[Abstract]

4 Chemical processing as a tool to generate ovalbumin variants with changed stability
article 2003    
Author: Kosters, H.A. · Broersen, K. · Groot, J.de · Simons, J.W.F.A. · Wierenga, P. · Jongh, H.H.J.de
Keywords: Nutrition · Food technology · Chemical processing · Modification · Ovalbumin · Structural integrity · Thermostability · Chemical modification · Differential scanning calorimetry · Fluorescence · Proteins · Thermodynamics · Chemical processing · Biotechnology · guanidine · ovalbumin · tryptophan · alkalinity · article · chemical procedures · covalent bond · denaturation · energy · lipophilicity · methylation · protein binding · protein folding · protein modification · protein processing · protein stability · spectroscopy · temperature dependence · thermodynamics · Animals · Chemical Industry · Chickens · Drug Stability · Hydrogen-Ion Concentration · Hydrophobicity · Ovalbumin · Protein Conformation · Protein Denaturation · Protein Folding · Protein Structure, Quaternary · Protein Structure, Secondary · Protein Structure, Tertiary · Temperature
[Abstract]

5 Glycoforms of β-Lactoglobulin with Improved Thermostability and Preserved Structural Packing
article 2004    
Author: Broersen, K. · Voragen, A.G.J. · Hamer, R.J. · Jongh, H.H.J. de
Keywords: Nutrition · Food technology · β-Lactoglobulin · Glycosylation · Maillard reaction · Monosaccharides · Thermal stability · Amines · Glucose · Hydrophobicity · Proteins · Thermodynamics · Structural stability · Thermostability · Biotechnology · beta lactoglobulin · amino acid sequence · analytic method · article · chemical modification · hydrophobicity · normal distribution · protein secondary structure · protein structure · protein tertiary structure · structure analysis · thermostability · Fructose · Glucose · Glycosylation · Hydrogen-Ion Concentration · Lactoglobulins · Macromolecular Substances · Protein Binding · Protein Conformation · Protein Denaturation · Protein Isoforms · Protein Structure, Quaternary · Protein Structure, Secondary · Protein Structure, Tertiary · Receptors, Fc · Temperature
[Abstract]

6 Legumin allergens from peanuts and soybeans: Effects of denaturation and aggregation on allergenicity
article 2008    
Author: Boxtel, E.L. van · Broek, L.A.M. van den · Koppelman, S.J. · Gruppen, H.
Keywords: Health · Ara h 3 · Food allergy · Glycinin · Heat processing · Pepsin digestion · Ara · Arachis hypogaea · Glycine max · allergen · allergen Ara h3 · globulin · glycinin · immunoglobulin E · legumin protein, plant · pepsin A · soybean protein · vegetable protein · article · blood · chemistry · drug stability · food allergy · heat · human · immunology · metabolism · peanut · peanut allergy · plant seed · protein denaturation · protein quaternary structure · soybean · structure activity relation · Allergens · Arachis hypogaea · Drug Stability · Food Hypersensitivity · Globulins · Heat · Humans · Immunoglobulin E · Peanut Hypersensitivity · Pepsin A · Plant Proteins · Protein Denaturation · Protein Structure, Quaternary · Seeds · Soybean Proteins · Soybeans · Structure-Activity Relationship · Healthy for Life · Healthy Living
[Abstract]

Search results also available in MS Excel format.

Showing 1 to 6 of 6 found. | Sort by date