Distinction between dry and raw milk using monoclonal antibodies prepared against dry milk proteins

Journal of Dairy Science

Volumn 87, Issue 8, 2004, Pages 2720-2729

  Chen, W L ^a   Huang, M T ^a   Liu, H C ^a   Li, C W ^a   Mao, S J T ^a  

^a NATIONAL CHIAO TUNG UNIVERSITY   (Taiwan)

Author keywords

Dry milk; Monoclonal antibody; Thermal denaturation; lactoglobulin

Indexed keywords

ANIMALIA;

EID: 4243163216     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(04)73399-8     Document Type: Article

References (43)

1. Anema, S. G., and Y. Li. 2003. Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect on casein micelle size. J. Dairy Res. 70:73-83.
2. Bertrand-Harb, C., A. Baday, M. Dalgalarrondo, J. M. Chobert, and T. Haertle. 2002. Thermal modifications of structure and codenaturation of alpha-lactalbumin and beta-lactoglobulin induce changes of solubility and susceptibility to proteases. Nahrung 46:283-289.
3. Carbonaro, M., S. Nicoli, and G. Musci. 1999. Heat-induced aggregation of Phaseolus vulgaris L. proteins: An electron spin resonance study. J. Agric. Food Chem. 47:2188-2192.
4. Chang, J. Y., and L. Li. 2001. The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: Fractionation of conformational isomers of alpha-lactalbumin. J. Biol. Chem. 276:9705-9712.
5. Cho, Y., W. Gu, S. Watkins, S. P. Lee, T. R. Kim, J. W. Brady, and C. A. Batt. 1994. Thermostable variants of bovine beta-lactoglobulin. Protein Eng. 7:263-270.
6. Cho, Y., H. Singh, and L. K. Creamer. 2003. Heat-induced interactions of beta-lactoglobulin A and kappa-casein B in a model system. J. Dairy Res. 70:61-71.
7. Clement, G., D. Boquet, Y. Frobert, H. Bernard, L. Negroni, J. M. Chatel, K. Adel-Patient, C. Creminon, J. M. Wal, and J. Grassi. 2002. Epitopic characterization of native bovine beta-lactoglobulin. J. Immunol. Methods 266:67-78.
8. Doi, H., M. Hiramatsu, F. Ibuki, and M. Kanamori. 1985. Gelation of the heat-induced complex between kappa-casein and alpha-lactalbumin. J. Nutr. Sci. Vitaminol. (Tokyo) 31:77-87.
9. Dutta, P. K., K. Hammons, B. Willibey, and M. A. Haney. 1991. Analysis of protein denaturation by high-performance continuous differential viscometry. J. Chromatogr. 536:113-121.
10. Havea, P., H. Singh, and L. K. Creamer. 2001. Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment. J. Dairy Res. 68:483-497.
11. Henry, G., D. Molle, F. Morgan, J. Fauquant, and S. Bouhallab. 2002. Heat-induced covalent complex between casein micelles and beta-lactoglobulin from goat's milk: Identification of an involved disulfide bond. J. Agric. Food Chem. 501:185-191.
12. Huang, G. S., S. P. Wang, W. T. Chang, T. J. Sun, S. C. Wang, R. Chu, and S. J. T. Mao. 1999. Intracellular processing generated MDA-lys epitope in foam cells. Life Sci. 65:285-296.
13. Jimenez-Guzman, J., A. E. Cruz-Guerrero, G. Rodriguez-Serrano, A. Lopez-Munguia, L. Gomez-Ruiz, and M. Garcia-Garibay. 2002. Enhancement of lactase activity in milk by reactive sulfhydryl groups induced by heat treatment. J. Dairy Sci. 85:2497-2502.
14. Kitabatake, N., R. Wada, and Y. Fujita. 2001. Reversible conformational change in beta-lactoglobulin A modified with N-ethylmaleimide and resistance to molecular aggregation on heating. J. Agric. Food Chem. 49:4011-4018.
15. Kobayashi, K., A. Hirano, A. Ohta, T. Yoshida, K. Takahashi, and M. Hattori. 2001, Reduced immunogenicity of beta-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight. J. Agric. Food Chem. 49:823-831.
16. Kuitunen, M., E. Savilahti, and A. Sarnesto. 1994a. Human alpha-lactalbumin and bovine beta-lactoglobulin absorption in infants. Allergy 49:354-360.
17. Kuitunen, M., E. Savilahti, and A. Sarnesto. 1994b. Human alpha-lactalbumin and bovine beta-lactoglobulin absorption in premature infants. Pediatr. Res. 35:344-347.
18. Mao, S. J. T., R. E. Kazmar, J. C. Silverfield, M. C. Alley, K. Kluge, and C. G. Fathman. 1982. Immunochemical properties of human low density lipoproteins as explored by monoclonal antibodies. Binding characteristics distinct from those of conventional serum antibodies. Biochim. Biophys. Acta 713:365-374.
19. Mao, S. J. T., and B. A. Kottke. 1980. Tween-20 increases the immunoreactivity of apolipoprotein A-I in plasma. Biochim. Biophys. Acta 620:447-453.
20. Mao, S. J. T., J. G. Patton, J. J. Badimon, B. A. Kottke, M. C. Alley, and A. D. Cardin. 1983. Monoclonal antibodies to human plasma low-density lipoproteins. I. Enhanced binding of 1251-labeled low-density lipoproteins by combined use of two monoclonal antibodies. Clin. Chem. 29:1890-1897.
21. Mao, S. J. T., A. E. Rechtin, and R. L. Jackson. 1988. Monoclonal antibodies that distinguish between active and inactive forms of human postheparin plasma hepatic triglyceride lipase. J. Lipid Res. 29:1023-1029.
22. Mao, S. J. T., A. E. Rechtin, J. L. Krstenansky, and R. L. Jackson. 1990. Characterization of a monoclonal antibody specific to the amino terminus of the alpha-chain of human fibrin. Thromb. Haemost. 63:445-448.
23. Marcovina, S., D. France, R. A. Phillips, and S. J. T. Mao. 1985a. Monoclonal antibodies can precipitate low-density lipoprotein. I. Characterization and use in determining apolipoprotein B. Clin. Chem. 31:1654-1658.
24. Marcovina, S., B. A. Kottke, and S. J. T. Mao. 1985b. Monoclonal antibodies can precipitate low-density lipoprotein. II. Radioimmunoassays with single and combined monoclonal antibodies for determining apolipoprotein B in serum of patients with coronary artery disease. Clin. Chem. 31:1659-1663.
25. Martinez-Torres, C., I. Leets, P. Taylor, J. Ramirez, M. del Valle Camacho, and M. Layrisse. 1986. Heme, ferritin and vegetable iron absorption in humans from meals denatured of heme iron during the cooking of beef. J. Nutr. 116:1720-1725.
26. Mine Y., and J. W. Zhang. 2002. Comparative studies on antigenicity and allergenicity of native and denatured egg white proteins. J. Agric. Food Chem. 509:2679-2683.
27. Morgan, F., A. Venien, S. Bouhallab, D. Molle, J. Leonil, G. Peltre, and D. Levieux. 1999. Modification of bovine beta-lactoglobulin by glycation in a powdered state or in an aqueous solution: Immunochemical characterization. J. Agric. Food Chem. 47:4543-4548.
28. Oldfield, D. J., H. Singh, M. W. Taylor, and K. N. Pearce. 1998. Kinetics of denaturation and aggregation of whey protein in skim milk heated in an ultra-high temperature (UHT) plant. Int. Dairy J. 8:311-318.
29. Papiz, M. Z., L. Sawyer, E. E. Eliopoulos, A. C. North, J. B. Findlay, R. Sivaprasadarao, T. A. Jones, M. E. Newcomer, and P. J. Kraulis. 1986. The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324:383-385.
30. Patton, J. G., J. J. Badimon, and S. J. T. Mao. 1983. Monoclonal antibodies to human plasma low-density lipoproteins. II. Evaluation for use in radioimmunoassay for apolipoprotein B in patients with coronary artery disease. Clin. Chem. 29:1898-1903.
31. Pfeil, W. 1998. Is the molten globule a third thermodynamic state of protein? The example of alpha-lactalbumin. Proteins 30:43-48.
32. Recio, I., and C. Olieman. 1996. Determination of denatured serum proteins in the casein fraction of heat-treated milk by capillary zone electrophoresis. Electrophoresis 17:1228-1233.
33. Relkin, P. 1996. Thermal unfolding of beta-lactoglobulin, alpha-lactalbumin, and bovine serum albumin. A thermodynamic approach. Crit. Rev. Food Sci. Nutr. 36:565-601.
34. Restani, P., A. Gaiaschi, A. Plebani, B. Beretta, G. Cavagni, A. Fiocchi, C. Poiesi, T. Velona, A. G. Ugazio, and C. L. Galli. 1999. Cross-reactivity between milk proteins from different animal species. Clin. Exp. Allergy 29:997-1004.
35. Sanchez, L., M. D. Perez, P. Puyol, M. Calvo, and G. Brett. 2002. Determination of vegetal proteins in milk powder by enzyme-linked immunosorbent assay: Interlaboratory study. J. AOAC Int. 85:1390-1397.
36. Selo, I., C. Creminon, J. Grassi, and J. Y. Couraud. 2002. Anti-allergen antibodies can be neutralized by antibodies obtained against a peptide complementary to the allergen: towards a new peptide therapy for allergy. Immunol. Lett. 80:133-138.
37. Sorva, R., S. Makinen-Kiljunen, and K. Juntunen-Backman. 1994. Beta-lactoglobulin secretion in human milk varies widely after cow's milk ingestion in mothers of infants with cow's milk allergy. J. Allergy Clin. Immunol. 93:787-792.
38. Steffensen, C. L., H. J. Andersen, and J. H. Nielsen. 2002. Aldehyde-induced xanthine oxidase activity in raw milk. J. Agric. Food Chem. 50:7392-7395.
39. Tsonev, L. I., and A. G. Hirsh. 2000. Fluorescence ratio intrinsic basis states analysis: A novel approach to monitor and analyze protein unfolding by fluorescence. J. Biochem. Biophys. Methods 45:1-21.
40. Turner, J. A., L. R. Sivasundaram, M. A. Ottenhof, I. A. Farhat, R. S. Linforth, and A. J. Taylor. 2002. Monitoring chemical and physical changes during thermal flavor generation. J. Agric. Food Chem. 50:5406-5411.
41. Valkonen, K. H., N. Marttinen, and T. Alatossava. 2001. Electrophoretic methods for fractionation of native and heat-denatured bovine beta-lactoglobulin. Bioseparation 10:145-152.
42. Venien, A., D. Levieux, C. Astier, L. Briand, J. M. Chobert, and T. Haertle. 1997. Production and epitopic characterization of monoclonal antibodies against bovine beta-lactoglobulin. J. Dairy Sci. 80:1977-1987.
43. Yang, S. J., and S. J. T. Mao. 1999. A simple HPLC purification procedure for porcine plasma haptoglobin. J. Chromatagr. B 731:395-402.