- 1) Price, K. R., Johnson, I. T., and Fenwick, G. R., The chemistry and biological significance of saponins in foods and feedingstuffs. CRC Crit. Rev. Food Sci. Nutr., 26, 27-135 (1987).
- 2) Ikedo, S., Shimoyamada, M., and Watanabe, K., Interaction between bovine serum albumin and saponin as studied by heat stability and protease digestion. J. Agric. Food Chem., 44, 792-795 (1996).
- 3) Shimoyamada, M., Ikedo, S., Ootsubo, R., and Watanabe, K., Effect of soybean saponins on chymotryptic hydrolyses of soybean proteins. J. Agric. Food Chem., 46, 4793-4797 (1998).
- . 1997. p. A25- A28.
- . 1982. p. 1- 59.
- 6) Papiz, M. Z., Sawyer, L., Eliopoulos, E. E., North, A. C. T., Findlay, J. B. C., Sivaprasadarao, R., Jones, T. A., Newcomer, M. E., and Kraulis, P. J., The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature (London), 324, 383-385 (1986).
- 7) Savilahti, E. and Kuitunen, M., Allergenicity of cow milk proteins. J. Pediatr., 121, S12-S20 (1992).
- 8) Wal, J.-M., An update on allergens Cow’s milk allergens. Allergy, 53, 1013-1022 (1998).
- 9) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685 (1970).
- 10) Shimoyamada, M., Yoshimura, H., Tomida, K., and Watanabe, K., Stabilities of bovine β-lactoglobulin/retinol or retinoic acid complexes against tryptic hydrolysis, heating and light-induced oxidation. Lebensm.-Wiss. u.-Technol., 29, 763-766 (1996).
- 11) Kuwajima, K., Harushima, Y., and Sugai, S., Influence of Ca2+ binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra. Int. J. Pept. Protein Res., 27, 18-27 (1986).
Bioscience, Biotechnology, and Biochemistry
Volume 64, 2000 - Issue 4