Reduced immunogenicity of β-lactoglobulin by single amino acid substitution
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M. Totsuka | M. Hattori | Kiyoshi Yamada | T. Yoshida | C. Kume | Asako Sachi | Fumiko Yuyama | Naoko Tomiyama | Rina Kodama
[1] Yao-Hsu Yang,et al. Analysis of α-lactalbumin-, β-lactoglobulin-, and casein-specific IgE among children with atopic diseases in a tertiary medical center in Northern Taiwan. , 2014, Journal of microbiology, immunology, and infection = Wei mian yu gan ran za zhi.
[2] M. Totsuka,et al. Down‐regulation of antigen‐specific antibody production by TCR antagonist peptides in vivo , 2000, European journal of immunology.
[3] R. Mäntyjärvi,et al. Allergy to lipocalins: a consequence of misguided T-cell recognition of self and nonself? , 1999, Immunology today.
[4] Y. Kohno,et al. Frequency of Immediate–Type Food Allergy in Children in Japan , 1999, International Archives of Allergy and Immunology.
[5] Darren R. Flower,et al. Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin , 1997 .
[6] M. Totsuka,et al. Antigen-specific inhibition of CD4+ T-cell responses to beta-lactoglobulin by its single amino acid-substituted mutant form through T-cell receptor antagonism. , 1997, Cytotechnology.
[7] S. Kaminogawa. Food allergy, oral tolerance and immunomodulation--their molecular and cellular mechanisms. , 1996, Bioscience, biotechnology, and biochemistry.
[8] D R Flower,et al. The lipocalin protein family: structure and function. , 1996, The Biochemical journal.
[9] Koji Takahashi,et al. Functional changes in β-lactoglobulin by conjugation with carboxymethyl dextran , 1994 .
[10] Y. Katakura,et al. Unfolding/refolding studies on bovine beta-lactoglobulin with monoclonal antibodies as probes. Does a renatured protein completely refold? , 1993, The Journal of biological chemistry.
[11] M. Totsuka,et al. Expression and Secretion of Bovine β-Lactoglobulin in Saccharomyces cerevisiae , 1990 .
[12] M. Totsuka,et al. Expression and secretion of bovine beta-lactoglobulin in Saccharomyces cerevisiae. , 1990, Agricultural and biological chemistry.
[13] R. Waniska,et al. Foaming and emulsifying properties of glycosylated beta-lactoglobulin , 1988 .
[14] D. Mulvihill,et al. Gelation characteristics of whey proteins and beta-lactoglobulin , 1987 .
[15] P. Kraulis,et al. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein , 1986, Nature.
[16] V. Fricová,et al. First experience with the use of the Pharmacia PhastSystem for the characterization of haemoglobins by isoelectric focusing. , 1986, Journal of chromatography.
[17] M. Saito,et al. Emulsifying and Structural Properties of β-Lactoglobulin at Different PHs , 1985 .
[18] U. Cogan,et al. Binding affinities of retinol and related compounds to retinol binding proteins. , 1976, European journal of biochemistry.
[19] J. Heller,et al. The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, -lactoglobulin, and the retinol-binding protein of human plasma. , 1972, The Journal of biological chemistry.
[20] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[21] H. Mckenzie,et al. On the fractionation of β-lactoglobulin and α-lactalbumin , 1967 .
[22] J. M. Armstrong,et al. On the fractionation of beta-lactoglobulin and alpha-lactalbumin. , 1967, Biochimica et biophysica acta.