Vai ai contenuti. | Spostati sulla navigazione | Spostati sulla ricerca | Vai al menu | Contatti | Accessibilità

| Crea un account

Battaglia, Francesca (2008) Analysis of Allergenic Proteins by Mass Spectrometry. [Tesi di dottorato]

Full text disponibile come:

[img]
Anteprima
Documento PDF
7Mb

Abstract (inglese)

The general aim of the activities conducted in the framework of my PhD were to learn modern techniques for analyzing proteins by mass spectrometry (MS) and then to apply these techniques and approaches to the analysis of allergenic proteins contained in foods. My research activities were conducted at the Laboratory of Protein Chemistry of CRIBI, University of Padua, where previously I have conducted the research for my Thesis for the Doctor degree in Pharmaceutical Biotechnologies. During the fist year of my PhD I have concluded the Thesis project on the amyloid aggregation of -lactalbumin, a model protein utilized for investigating molecular aspects of protein amyloidogenesis. The results of this research were quite interesting and indeed they have been published in an international journal.
During the first two years I acquired a solid knowledge on several aspects of the MS methodology and I was able to learn the theory and practice of several modern techniques and approaches in this ambit. The specific aim was to analyze allergenic proteins contained in complex matrices as foods and to this aim several proteins were extracted and purified from
several food samples. The research has been focused mostly on the allergenic proteins from milk and eggs, known to cause widespread allergies. The proteins of interest were analyzed by using several chromatographic and electrophoretic techniques and also by means of HPLC connected to a tandem MS electrospray instrument. I was able to show that MS techniques
can be used to identify allergenic proteins even when contained in very complex mixtures. Therefore, these MS techniques perhaps can be used as an alternative to the immunochemical
methods nowadays in use for detecting allergens. I have also analyzed the chemical modifications that allergenic proteins suffer during several industrial treatments of foods,
including heat treatment.
During the third year of my PhD I spent a six months period at the Biochemistry Laboratory of the Imperial College in London, being involved in a project aimed to study in a large scale the proteins of the mosquito Anopheles gambiae. The MS analyses were focused on the proteins responsible of the mating behaviour of A. gambiae, hoping to identify a target for controlling the behaviour of this vector of the malaria disease.
Summing up, besides the publication dealing with amyloid aggregates of beta- lactalbumin, this PhD Thesis is composed by a major part dealing with MS analysis of allergenic proteins and by a minor one dealing with MS analysis of proteins from A. gambiae.


Statistiche Download - Aggiungi a RefWorks
Tipo di EPrint:Tesi di dottorato
Relatore:Fontana, Angelo
Dottorato (corsi e scuole):Ciclo 20 > Scuole per il 20simo ciclo > BIOCHIMICA E BIOTECNOLOGIE > BIOTECNOLOGIE
Data di deposito della tesi:2008
Anno di Pubblicazione:2008
Parole chiave (italiano / inglese):mass spectrometry, protein allergen, LC-MS/MS
Settori scientifico-disciplinari MIUR:Area 05 - Scienze biologiche > BIO/10 Biochimica
Struttura di riferimento:Centri > Centro di ricerca Interdipartimentale Biotecnologie Innovative (CRIBI)
Codice ID:633
Depositato il:23 Ott 2008
Simple Metadata
Full Metadata
EndNote Format

Bibliografia

I riferimenti della bibliografia possono essere cercati con Cerca la citazione di AIRE, copiando il titolo dell'articolo (o del libro) e la rivista (se presente) nei campi appositi di "Cerca la Citazione di AIRE".
Le url contenute in alcuni riferimenti sono raggiungibili cliccando sul link alla fine della citazione (Vai!) e tramite Google (Ricerca con Google). Il risultato dipende dalla formattazione della citazione.

1. Ahmed N., Mirshekar-Syahkal B., Kennish L., Karachalias N., Babaei-Jadidi R. and Thornalley P.J. (2005). Assay of advanced glycation endproducts in selected beverages and food by liquid chromatography with tandem mass spectrometric detection. Mol. Nutr. Food Res. 49, 691–699. Cerca con Google

2. Ahmed N. and Thornalley P.J. (2002). Chromatographic assay of glycation adducts in human serum albumin glycated in vitro by derivatization with 6-aminoquinolyl-Nhydroxysuccinimidyl- carbamate and intrinsic fluorescence. Biochem. J. 364, 15–24. Cerca con Google

3. Andersen C.M., Vishart M. and Holm V.K. (2005). Application of fluorescence spectroscopy in the evaluation of light-induced oxidation in cheese. J. Agric. Food Chem. 53, 9985–9992. Cerca con Google

4. Ankrah N.A. and Appiah-Opong R. (1999). Toxicity of low levels of methylglyoxal: depletion of blood glutathione and adverse effect on glucose tolerance in mice. Toxicol. Lett. 109, 61–67. Cerca con Google

5. Baisier, W.M. and Labuza, T.P. (1992). Maillard browning kinetics in a liquid model system. J. Agric. Food Chem., 40, 707–713. Cerca con Google

6. Bando N., Tsuji H., Hiemori M., Yoshizumi K., Yamanishi R., Kimoto M. and Ogawa T. (1998). Quantitative analysis of Gly m Bd 28K in soybean products by a sandwich enzymelinked immunosorbent assay. J. Nutr. Sci. Vitaminol. 44, 655-664. Cerca con Google

7. Besler M. and Steinhart H., Paschke A. (2001). Stability of food allergens and allergenicity of processed foods. J. Chromatogr. B Biomed. Sci. Appl. 756, 207–228. Cerca con Google

8. Biemann K. (1992). Mass spectrometry of peptides and proteins. Annu. Rev. Biochem. 61, 977–1010. Cerca con Google

9. Birlouez-Aragon I., Leclere J., Quedraogo C.L., Birlouez E. and Grongnet J.F. (2001). The FAST method, a rapid approach of the nutritional quality of heat-treated foods. Nahrung. 45, 201-205. Cerca con Google

10. Bischoff S.C., Mayer J.H. and Manns M.P. (2000). Allergy and the gut. Int. Arch. Allergy Immunol. 121,270–283. Cerca con Google

11. Boccagni P., Favari F., Zanoni G., Pezzini A. and Tridente G. (1994). Comparison of four in vitro assays for specific IgE detection. Int. J. Clin. Lab. Res. 24, 102–105. Cerca con Google

12. Bradford M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Annal. Biochem. 72, 248– 254. Cerca con Google

13. Breiteneder H. and Radauer C. (2004). A classification of plant food allergens. J. Allergy. Clin. Immunol. 113, 821-830. Cerca con Google

14. Breiteneder H. and Mills E.N. (2005). Molecular properties of food allergens. J. Allergy Clin. Immunol. 115, 14–23. Cerca con Google

15. Bucala R., Mitchell R., Arnold K., Innerarity T., Vlassara H. and Cerami A. (1995). Identification of the major site of apolipoprotein B modification by advanced glycosylation end products blocking uptake by the low density lipoprotein receptor. J. Biol. Chem. 270, 10828–10832. Cerca con Google

16. Burks, A.W., Cockvell, G., Connaughton, C., and Helm and R.M. (1994). Epitope specificity and immunoaffinity purification of the major peanut allergen Ara h1. J. Allergy Clin. Immunol. 93, 743–750. Cerca con Google

17. Businco L., Bruno G. and Giampietro P.G. (1999). Prevention and management of food allergy. Acta Paediatr. Suppl. 88, 104–109. Cerca con Google

18. Cordle C.T. (2004). Soy protein allergy: incidence and relative severity. J. Nutr. 134, 1213– 1219. Cerca con Google

19. Coussons P.J., Jacoby J., McKay A., Kelly S.M., Price N.C. and Hunt J.V. (1997). Glucose modification of human serum albumin: a structural study. Free Radic. Biol. Med. 22, 1217– 1227. Cerca con Google

20. Czerwenka C., Maier I., Pittner F. and Lindner W. (2006). Investigation of the lactosylation of whey proteins by liquid chromatography-mass spectrometry. J. Agric. Food Chem. 54, 8874–8882. Cerca con Google

21. David T.J. (2000). Adverse reactions and intolerance to foods. Br. Med. Bull. 56, 34–50. Cerca con Google

22. Davis P.J., Smales C.M. and James D.C. (2001). How can thermal processing modify the antigenicity of proteins? Allergy. 56, 56–60. Cerca con Google

23. Docena G., Rozenfeld P., Fernández R. and Fossati C.A. (2002). Evaluation of the residual antigenicity and allergenicity of cow's milk substitutes by in vitro tests. Allergy. 57, 83–91. Cerca con Google

24. Docena G.H., Fernandez R., Chirdo F.G. and Fossati C.A. (1996). Identification of casein as the major allergenic and antigenic protein of cow's milk. Allergy. 51, 412–416. Cerca con Google

25. Ehn B.M., Allmere T., Telemo E., Bengtsson U. and Ekstrand B.(2005). Modification of IgE binding to beta-lactoglobulin by fermentation and proteolysis of cow's milk. J. Agric. Food Chem. 53, 3743–3748. Cerca con Google

26. Elsayed S., Hill D.J. and Do T.V. (2004). Evaluation of the allergenicity and antigenicity of bovine-milk alphas1-casein using extensively purified synthetic peptides. Scand. J. Immunol. 60, 486–493. Cerca con Google

27. Erbersdobler H.F. and Somoza V. (2007). Forty years of furosine - forty years of using Maillard reaction products as indicators of the nutritional quality of foods. Mol. Nutr. Food Res. 51, 423–430. Cerca con Google

28. Farrell H.M. Jr., Qi P.X., Wickham E.D. and Unruh J.J. (2002). Secondary structural studies of bovine caseins: structure and temperature dependence of beta-casein phosphopeptide (1- 25) as analyzed by circular dichroism, FTIR spectroscopy, and analytical ultracentrifugation. J. Protein Chem. 21, 307–321. Cerca con Google

29. Fay L.B. and Brevard H. (2005). Contribution of mass spectrometry to the study of the Maillard reaction in food. Mass Spectrom. Rev. 24, 487–507. Cerca con Google

30. Fenn J.B., Mann M., Meng C.K., Wong S.F. and Whitehouse C.M. (1989). Electrospray ionization for mass spectrometry of large biomolecules. Science 246, 64–71. Cerca con Google

31. Ferreira F., Hawranek T., Gruber P., Wopfner N. and Mari A. (2004). Allergic crossreactivity: from gene to the clinic. Allergy. 59, 243–267. Cerca con Google

32. Ferrer E., Alegría A., Farré R., Abellán P. and Romero F. (2000). Effects of thermal processing and storage on available lysine and furfural compounds contents of infant formulas. J. Agric. Food Chem. 48, 1817–1822. Cerca con Google

33. Fogliano V., Monti S.M., Visconti A., Randazzo G., Facchiano A.M., Colonna G. and Ritieni A. (1998). Identification of a beta-lactoglobulin lactosylation site. Biochim. Biophys. Acta 1388, 295–304. Cerca con Google

34. Fu M.X., Requena J.R., Jenkins A.J., Lyons T.J., Baynes J.W. and Thorpe S.R. (1996). The advanced glycation end product, Nepsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions. J. Biol. Chem. 271, 9982–9986. Cerca con Google

35. Fujita M., Baba R., Shimamoto M., Sakuma Y. and Fujimoto S. (2007). Molecular morphology of the digestive tract; macromolecules and food allergens are transferred intact across the intestinal absorptive cells during the neonatal-suckling period. Med. Mol. Morphol. 40, 1–7. Cerca con Google

36. Galvani M., Hamdan M., Herbert B. and Righetti P.G. (2001). Alkylation kinetics of proteins in preparation for two-dimensional maps: a matrix assisted laser desorption/ionization-mass spectrometry investigation. Electrophoresis. 22, 2058–2065. Cerca con Google

37. Gerrard J.A., Meade S.J., Miller A.G., Brown P.K., Yasir S.B., Sutton K.H. and Newberry M.P. (2005). Protein cross-linking in food. Ann. N. Y. Acad. Sci. 1043, 97–103. Cerca con Google

38. Gómez-Ollés S., Cruz M.J., Renström A., Doekes G., Morell F. and Rodrigo M.J. (2006). An amplified sandwich EIA for the measurement of soy aeroallergens. Clin. Exp. Allergy. 36, 1176–1183. Cerca con Google

39. Hanash S. (2003). Disease proteomics. Nature 422, 226–232. Cerca con Google

40. Hasenkopf K., Rönner B., Hiller H. and Pischetsrieder M. (2002). Analysis of glycated and ascorbylated proteins by gas chromatography-mass spectrometry. J. Agric. Food Chem. 50, 5697–5703. Cerca con Google

41. Heddleson R.A., Park O. and Allen J.C. (1997). Immunogenicity of casein phosphopeptides derived from tryptic hydrolysis of beta-casein. J. Dairy Sci. 80, 1971–1976. Cerca con Google

42. Hiemori M., Bando N., Ogawa T., Shimada H., Tsuji H., Yamanishi R. and Terao J. (2000). Occurrence of IgE antibody-recognizing N-linked glycan moiety of a soybean allergen, Gly m Bd 28K. Int. Arch. Allergy Immunol. 122, 238–245. Cerca con Google

43. Humeny A., Kislinger T., Becker C.M. and Pischetsrieder M. (2002). Qualitative determination of specific protein glycation products by matrix-assisted laser desorption/ionization mass spectrometry Peptide mapping. J. Agric. Food Chem. 50, 2153– 2160. Cerca con Google

44. Ikeda K., Nagai R., Sakamoto T., Sano H., Araki T., Sakata N., Nakayama H., Yoshida M., Ueda S. and Horiuchi S. (1998). Immunochemical approaches to AGE-structures: characterization of anti-AGE antibodies. J. Immunol. Methods. 215, 95–104. Cerca con Google

45. Kasai N. and Ikehara H. (2005). Stepwise extraction of proteins and carbohydrates from soybean seed. J. Agric. Food Chem. 53, 4245–4252. Cerca con Google

46. Kato Y., Watanabe H. and Matsuda T. (2000). Ovomucoid rendered insoluble by heating with wheat gluten but not with milk casein. Biosci. Biotechnol. Biochem. 64, 198-201. Cerca con Google

47. Koppelman, S. J., Bruijnzeel-Koomen, C.A., Hessing, M. and de Jongh, H.H. (1999). Heatinduced conformational changes of Ara h1, a major peanut allergen, do not affect its allergenic properties. J. Biol. Chem. 274, 4770–4777. Cerca con Google

48. Kopper R.A., Odum N.J., Sen M., Helm R.M., Steve Stanley J. and Wesley Burks A. (2004). Peanut protein allergens: gastric digestion is carried out exclusively by pepsin. J. Allergy Clin. Immunol. 114, 614–618. Cerca con Google

49. Krause R., Kühn J., Penndorf I., Knoll K. and Henle T. (2004). N-Terminal pyrazinones: a new class of peptide-bound advanced glycation end-products. Amino Acids. 27, 9–18. Cerca con Google

50. Kumosinski T.F., Brown E.M. and Farrell H.M. Jr. (1991). Three-dimensional molecular modeling of bovine caseins: kappa-casein. J. Dairy Sci. 74, 2879–8287. Cerca con Google

51. Lane C.S. (2005). Mass spectrometry-based proteomics in the life sciences. Cell Mol. Life Sci. 62, 848–869. Cerca con Google

52. L'Hocine L., Boye J.I. and Munyana C. (2007). Detection and quantification of soy allergens in food: study of two commercial enzyme-linked immunosorbent assays. J. Food Sci. 72, 145–153. Cerca con Google

53. Lo T.W., Westwood M.E., McLellan A.C., Selwood T. and Thornalley P.J. (1994). Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with Nalpha-acetylarginine, Nalpha-acetylcysteine and Nalpha-acetyllysine and bovine serum albumin. J. Biol. Chem. 269, 32299–32305. Cerca con Google

54. Luz Sanz M., Corzo-Martínez M., Rastall R. A., Olano A. and Moreno F.J. (2007). Characterization and in vitro digestibility of bovine _-lactoglobulin glycated with galactooligosaccharides. J. Agric. Food Chem. 55, 7916–7925. Cerca con Google

55. Maleki, S. J., Chung, S. Y, Champagne, E. T, and Raufman, J. P. (2000). The effects of roasting on the allergenic properties of peanut proteins. J. Allergy Clin. Immunol. 106, 763– 768. Cerca con Google

56. Malin E.L., Brown E.M., Wickham E.D. and Farrell H.M. Jr. (2005). Contributions of terminal peptides to the associative behaviour of _1-casein. J. Dairy Sci. 88, 2318–2328. Cerca con Google

57. Marvin L.F., Parisod V., Fay L.B. and Guy P.A. (2002). Characterization of lactosylated proteins of infant formula powders using two-dimensional gel electrophoresis and nanoelectrospray mass spectrometry. Electrophoresis. 23, 2505–2512. Cerca con Google

58. Miller A.G. and Gerrard J.A. (2005). Assessment of protein function following cross-linking by alpha-dicarbonyls. Ann. N. Y. Acad. Sci. 1043, 195–200. Cerca con Google

59. Mills E.N. and Breiteneder H. (2005). Food allergy and its relevance to industrial food proteins. Biotechnol. Adv. 23, 409-414. Cerca con Google

60. Minikiewicz P., Slangen C.J., Lagerwerf F.M., Haverkamp J., Rollema H.S. and Visser S. (1996). Reversed-phase high-performance liquid chromatographic separation of bovine kappa-casein macropeptide and characterization of isolated fractions. J. Chromatogr. A. 743, 123–135. Cerca con Google

61. Monaci L. and van Hengel A.J. (2007). Effect of heat treatment on the detection of intact bovine beta-lactoglobulins by LC mass spectrometry. J. Agric. Food Chem. 55, 2985–2992. Cerca con Google

62. Morales F., J., Romero C. and Jimenez-Perez S., (1996). Evaluation of heat-induced changes in Spanish commercial milk: hydroxymethylfurfural and available lysine content. Int. J. of Food Sci. Tech. 31, 411-418. Cerca con Google

63. Morales F.J., Romero C. and Jiménez-Pérez S. (1997). Chromatographic determination of bound hydroxymethylfurfural as an index of milk protein glycosylation. J. Agric. Food Chem. 45, 1570–1573. Cerca con Google

64. Natale M., Bisson C., Monti G., Peltran A., Garoffo L.P., Valentini S., Fabris C., Bertino E., Coscia A. and Conti A. (2004). Cow's milk allergens identification by two-dimensional immunoblotting and mass spectrometry. Mol. Nutr. Food Res. 48, 363–369. Cerca con Google

65. Newkirk M.M., Goldbach-Mansky R., Lee J., Hoxworth J., McCoy A., Yarboro C., Klippel J. and El-Gabalawy H.S. (2003). Advanced glycation end-product (AGE)-damaged IgG and IgM autoantibodies to IgG-AGE in patients with early synovitis. Arthritis Res. Ther. 5, 82–90. Cerca con Google

66. Nielsen H.K., De Weck D., Finot P.A., Liardon R. and Hurrell R.F. (1985). Stability of tryptophan during food processing and storage. 1. Comparative losses of tryptophan, lysine and methionine in different model systems. Br. J. Nutr. 53, 281–292. Cerca con Google

67. Odani H., Shinzato T., Usami J., Matsumoto Y., Brinkmann Frye E., Baynes J.W. and Maeda K. (1998). Imidazolium crosslinks derived from reaction of lysine with glyoxal and methylglyoxal are increased in serum proteins of uremic patients: evidence for increased oxidative stress in uremia. FEBS Lett. 427, 381–385. Cerca con Google

68. Oya T., Hattori N., Mizuno Y., Miyata S., Maeda S., Osawa T. and Uchida K. (1999). Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts. J. Biol. Chem. 274, 18492–18502. Cerca con Google

69. Parker E.A., Donato L. and Dalgleish D.G. (2005). Effects of added sodium caseinate on the formation of particles in heated milk. J. Agric. Food Chem. 53, 8265–8272. Cerca con Google

70. Perkins D.N., Pappin D.J., Creasy D.M. and Cottrell J.S. (1999). Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis. 20, 3551–3567. Cerca con Google

71. Peterson C.G., Hansson T., Skott A., Bengtsson U., Ahlstedt S. and Magnussons J. (2007). Detection of local mast-cell activity in patients with food hypersensitivity. J. Investig. Allergol. Clin. Immunol. 17, 314–320. Cerca con Google

72. Peterson P.A. and Rask L. (1971). Studies on the fluorescence of the human vitamin Atransporting plasma protein complex and its individual components. J. Biol. Chem. 246, 7544–7550. Cerca con Google

73. Phizicky E., Bastiaens P.I., Zhu H., Snyder M. and Fields S. (2003). Protein analysis on a proteomic scale. Nature 422, 208–215. Cerca con Google

74. Plaza-Martín A.M., Jiménez-Feijoo R., Andaluz C., Giner-Muñoz M.T., Martin-Mateos M.A., Piquer-Gibert M. and Sierra-Martínez J.I. (2007). Polysensitization to aeroallergens and food in eosinophilic esophagitis in a pediatric population. Allergol. Immunopathol. 35, 35–37. Cerca con Google

75. Ring J., Brockow K. (2002). Adverse drug reactions: mechanisms and assessment. Eur. Surg. Res. 34, 170–175. Cerca con Google

76. Roepstorff P. and Fohlman J. (1984). Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 11, 601. Cerca con Google

77. Roychaudhuri R., Sarath G., Zeece M. and Markwell J. (2004). Stability of the allergenic soybean Kunitz trypsin inhibitor. Biochim. Biophys. Acta. 1, 207–212. Cerca con Google

78. Rupa P. and Mine Y. (2003). Immunological comparison of native and recombinant egg allergen, ovalbumin, expressed in Escherichia coli. Biotechnol. Lett. 25, 1917–1924. Cerca con Google

79. Rytkönen J., Valkonen K.H., Virtanen V., Foxwell R.A., Kyd J.M., Cripps A.W. and Karttunen T.J. (2006). Enterocyte and M-cell transport of native and heat-denatured bovine beta-lactoglobulin: significance of heat denaturation. J. Agric. Food Chem. 54, 1500–1507. Cerca con Google

80. Sali A., Glaeser R., Earnest T. and Baumeister W. (2003). From words to literature in structural proteomics. Nature 422, 216–225. Cerca con Google

81. Scaloni A., Perillo V., Franco P., Fedele E., Froio R., Ferrara L. and Bergamo P. (2002). Characterization of heat-induced lactosylation products in caseins by immunoenzymatic and mass spectrometric methodologies. Biochim. Biophys. Acta. 1598, 30–39. Cerca con Google

82. Schmitt A., Gasic-Milenkovic J. and Schmitt J. (2005). Characterization of advanced glycation end products: mass changes in correlation to side chain modifications. Anal. Biochem. 346, 101–106. Cerca con Google

83. Schmitt A., Schmitt J., Münch G. and Gasic-Milencovic J. (2005). Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics. Anal. Biochem. 338, 201-215. Cerca con Google

84. Sedmark J.J. and Grossberg SE (1977). A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Anal Biochem. 79, 544–552. Cerca con Google

85. Seiquer I., Díaz-Alguacil J., Delgado-Andrade C., López-Frías M., Muñoz Hoyos A., Galdó G. and Navarro M.P. (2006). Diets rich in Maillard reaction products affect protein digestibility in adolescent males aged 11-14 y. Am. J. Clin. Nutr. 83, 1082–1088. Cerca con Google

86. Sharma S., Kumar P., Betzel C. and Singh T.P. (2001). Structure and function of proteins involved in milk allergies. J. Chromatogr. B Biomed. Sci. Appl. 756, 183-187. Cerca con Google

87. Shin, D. S., Compadre, C. M., Maleki, S. J., Kopper, R. A., Sampson, H., Huang, S. K., Burks, A. W. and Bannon, G. A. (1998). Biochemical and structural analysis of the IgE binding sites on Ara h1, an abundant and highly allergenic peanut protein. J. Biol. Chem. 22, 13753–13759. Cerca con Google

88. Sicherer S.H., Morrow E.H. and Sampson H.A. (2000). Dose-response in double-blind, placebo-controlled oral food challenges in children with atopic dermatitis. J. Allergy Clin. Immunol. 105, 582–586. Cerca con Google

89. Sicherer S.H. and Sampson H.A. (2007). Peanut allergy: emerging concepts and approaches for an apparent epidemic. J. Allergy Clin. Immunol. 120, 491-503. Cerca con Google

90. Siciliano R., Rega B., Amoresano A. and Pucci P. (2000). Modern mass spectrometric methodologies in monitoring milk quality. Anal Chem. 72, 408–415. Cerca con Google

91. Skripak J.M., Matsui E.C., Mudd K. and Wood R.A. (2007). The natural history of IgEmediated cow's milk allergy. J. Allergy Clin. Immunol. 120, 1172–1177. Cerca con Google

92. Smyth E., Clegg R.A. and Holt C. (2004). A biological perspective on the structure and function of caseins and casein micelles Int. J. Dairy Technol. 57, 121–126. Cerca con Google

93. Sun H.S., Hill Park J. and Won K.S. (2007). Determination of proteins in infant formula by high-performance liquid chromatography–electrospray tandem mass spectrometry J. Chromatography B. 845, 69–73. Cerca con Google

94. Takagi K., Teshima R., Okunuki H., Itoh S., Kawasaki N., Kawanishi T., Hayakawa T., Kohno Y., Urisu A. and Sawada J. (2005). Kinetic analysis of pepsin digestion of chicken egg white ovomucoid and allergenic potential of pepsin fragments. Int. Arch. Allergy Immunol. 136, 23–32. Cerca con Google

95. Tatsumi E. and Hirose M. (1997). Highly ordered molten globule-like state of ovalbumin at acidic pH: native-like fragmentation by protease and selective modification of Cys367 with dithiodipyridine. J. Biochem. 122, 300–308. Cerca con Google

96. Teufel M., Biedermann T., Rapps N., Hausteiner C., Henningsen P., Enck P. and Zipfel S. (2007). Psychological burden of food allergy. World J. Gastroenterol. 13, 3456-3465. Cerca con Google

97. Thornalley P.J. (2005). Measurement of protein glycation, glycated peptides and glycation free adducts. Perit. Dial. Int. 25, 522–533. Cerca con Google

98. Tyers M. and Mann M. (2003). From genomics to proteomics. Nature 422, 193–197. Cerca con Google

99. Uchida K., Khor O.T., Oya T., Osawa T., Yasuda Y. and Miyata T. (1997). Protein modification by a Maillard reaction intermediate methylglyoxal. Immunochemical detection of fluorescent 5-methylimidazolone derivatives in vivo. FEBS Lett. 410, 313-318. Cerca con Google

100. Urisu A., Ando H., Morita Y., Wada E., Yasaki T., Yamada K., Komada K., Torii S., Goto M. and Wakamatsu T. (1997). Allergenic activity of heated and ovomucoid-depleted egg white. J. Allergy Clin. Immunol. 100, 171-176. Cerca con Google

101. Van der Plancken I., Van Remoortere M., Van Loey A. and Hendrickx M.E. (2004). Trypsin inhibition activity of heat-denatured ovomucoid: a kinetic study. Biotechnol. Prog. 20, 82-86. Cerca con Google

102. van Ree R. (2004). Clinical importance of cross-reactivity in food allergy. Curr. Opin. Allergy Clin. Immunol. 4, 235-240. Cerca con Google

103. Vieths S., Scheurer S. and Ballmer-Weber B. (2002). Current understanding of crossreactivity of food allergens and pollen. Ann. N. Y. Acad. Sci. 964, 47-68. Cerca con Google

104. Viquez, O. M., Konan, K. N. and Dodo, H. W. (2003). Structure and organization of the major peanut allergene Ara h1. Mol. Immunol. 40, 565–571. Cerca con Google

105. Wal J. M. (2004). Bovine milk allergenicity. Ann. Allergy Asthma Immunol. 93, S2–11. Cerca con Google

106. Xiang P., Haas E.J., Zeece M.G., Markwell J. and Sarath G. (2004). C-Terminal 23 kDa polypeptide of soybean Gly m Bd 28 K is a potential allergen. Planta 22, 56–63. Cerca con Google

107. Yoshino K., Sakai K., Mizuha Y., Shimizuike A. and Yamamoto S. (2004). Peptic digestibility of raw and heat-coagulated hen's egg white proteins at acidic pH range. Int. J. Food Sci. Nutr. 55, 635–640. Cerca con Google

108. Zhu H., Bilgin M. and Snyder M. (2003). Proteomics. Annu. Rev. Biochem. 72, 783–812. Cerca con Google

Download statistics

Solo per lo Staff dell Archivio: Modifica questo record