- 1) Nastasi, A., Mammina, C., Piersante, G. P., Robertazzo, M., and Caruso, P., A foodborne outbreak of Salmonella enteritidis vehicled by duck and hen eggs in southern Italy. New Microbiol., 21, 93-6 (1998).
- 2) Doyle, M. P., Escherichia coli O157:H7 and its significance in foods. Int. J. Food Microbiol., 12, 289-301 (1991).
- 3) Cassin, M. H., Lammerding, A. M., Todd, E. C., Ross, W., and McColl, R. S., Quantitative risk assessment for Escherichia coli O157:H7 in ground beef hamburgers. Int. J. Food Microbiol., 41, 21-44 (1998).
- 4) Tauxe, R. V., Foodborne illnesses. Strategies for surveillance and prevention. Lancet, 352, 19-26 (1998).
- 5) Smith, J. L., Foodborne illness in the elderly. J. Food Prot., 61, 1229-39 (1998).
- 6) Farkas, J., Irradiation as a method for decontaminating food. Int. J. Food Microbiol., 44, 189-204 (1998).
- 7) Thayer, D. W. and Boyd, G., Elimination of Escherichia coli O157:H7 in meats by gamma irradiation. Appl. Environ. Microbiol., 59, 1030-4 (1993).
- 8) Clavero, M. R., Monk, J. D., Beuchat, L. R., Doyle, M. P., and Brackett, R. E., Inactivation of Escherichia coli O157:H7, salmonellae, and Campylobacter jejuni in raw ground beef by gamma irradiation. Appl. Environ. Microbiol., 60, 2069-75 (1994).
- . 1991. p. 1- 18.
- 10) Savagaon, K. A., Venugopal, V., Kamat, S. V., Kumta, U. S., and Sreenivasan, A., Radiation preservation of tropical shrimp for ambient temperature storage. J. Food Sci., 37, 148-150 (1972).
- 11) Griffith, G., Irradiated foods: new technology, old debate. Trends Food Sci. Technol., 3, 251-252 (1992).
- 12) Thakur, B. R. and Singh, R. K., Combination processes in food irradiation. Trends Food Sci. Technol., 6, 7-11 (1995).
- 13) Rumbo, M., Chirdo, F. G., Fossati, C. A., and Anon, M. C., Analysis of structural properties and immunochemical reactivity of heat-treated ovalbumin. J. Agric. Food Chem., 44, 3793-98 (1996).
- 14) Ikura, K., Higashiguchi, F., Kitabatake, N., Doi, E., Narita, H., and Sasaki, R., Thermally induced epitope regions of ovalbumin identified with monoclonal antibodies. J. Food. Sci., 57, 635-639 (1992).
- 15) Kume, T., Ishii, T., and Matsuda, T., Immunochemical identification of irradiated chicken eggs. J. Sci. Food Agric., 65, 1-4 (1994).
- 16) Karlsson, R., Michaelsson, A., and Mattsson, L., Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor-based analytical system. J. Immunol. Methods, 145, 229-240 (1991).
- 17) Altschuh, D., Dubs, M.-C., Weiss, E., Zeder-Lutz, G., and Van Regenmortel, M. H. V., Determination of kinetic constants for the interaction between a monoclonal antibody and peptides using surface plasmon resonance. Biochemistry, 31, 6298-6304 (1992).
- 18) Wohlhueter, R. M., Parekh, K., Udhayakumar, V., Fang, S., and Lal, A. A., Analysis of binding of monoclonal antibody to a malarial peptide by surface plasmon resonance biosensor and integrated rate equations. J. Immunol., 153, 181-189 (1994).
- 19) Johne, B., Gadnall, M., and Hansen, K., Epitope mapping and binding kinetics of monoclonal antibodies studied by real time biospecific interaction analysis using surface plasmon resonance. J. Immunol. Methods, 160, 191-198 (1993).
- 20) Allauzen, S., Mani, J. C., Granier, C., Pau, B., and Bouanani, M., Epitope mapping and binding analysis of insulin-specific monoclonal antibodies using a biosensor approach. J. Immunol. Methods, 183, 27-32 (1995).
- 21) Björquist, P., Ehnebom, J., Inghardt, T., and Deinum, J., Epitopes on plasminogen activator inhibitor type-1 important for binding to tissue plasminogen activator. Biochim. Biophys. Acta, 1341, 87-98 (1997).
- 22) Sörensen, S. P. L. and Höyrup, M., Studies on proteins. I. On the preparation of egg-albumin solutions of well-defined composition, and on the analytical methods used. Compt. Rend. Trav. Lab. Carlsberg., 12, 12-67 (1915).
- 23) Köhler, G. and Milstein, C., Continuous cultures of fused cells secreting antibody of predefined specificity. Nature, 256, 495-7 (1975).
- 24) O’Shannessy, D. J., Brigham-Burke, M., Soneson, K. K., Hensley, P., and Brooks, I., Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: Use of nonlinear least-square analysis methods. Anal. Biochem., 212, 457-468 (1993).
- 25) Sanderson, D. C. W., Slater, C., and Cairns, K. J., Detection of irradiated food. Nature, 340, 23-24 (1989).
- 26) Dodd, N. J., Lea, J. S., and Swallow, A. J., ESR detection of irradiated food. Nature, 334, 387 (1988).
- 27) Stewart, E. M., Stevenson, M. H., and Gray, R., The effect of irradiation dose and storage time on the ESR signal in the cuticle of different components of the exoskeleton of Norway lobster (Nephrops norvegicus). Appl. Radiat. Isot., 44, 433-7 (1993).
- 28) Stevenson, M. H., Crone, A. V. J., and Hamilton, J. T. G., Irradiation detection. Nature, 344, 202-203 (1990).
- 29) Kaminogawa, S., Shimizu, M., Ametani, A., Hattori, M., Ando, O., Hachimura, S., Nakamura, Y., Totsuka, M., and Yamada, K., Monoclonal antibodies as probes for monitoring the denaturation process of bovine ß-lactoglobulin. Biochim. Biophys. Acta, 998, 50-56 (1989).
- 30) Kato, A., Shimizu, T., and Saga, S., Conformational changes in mutant lysozymes detected with monoclonal antibody. FEBS Lett., 371, 17-20 (1995).
- 31) Varshney, G. C., Mahana, W., Filloux, A. M., Venien, A., and Paraf, A., Structure of native and heat-denatured ovalbumin as revealed by monoclonal antibodies: Epitopic changes during heat treatment. J. Food Sci., 56, 224-227 (1991).
- 32) Huber, R. and Carrell, R. W., Implications of the three-dimensional structure of α1-antitrypsin for structure and function of serpins, Biochemistry, 28, 8951-8966 (1989).
Bioscience, Biotechnology, and Biochemistry
Volume 64, 2000 - Issue 4