Reduced immunogenicity of β-lactoglobulin by single amino acid substitution

[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.