Biochemical Journal · 1992 · 161 citations · 20 references
Life SciencesBiochemistryImmunologyAllergyHypersensitivityMolecular ImmunologyAllergic DiseaseFood AllergensFood AllergyIge-mediated AllergyImmunoglobulin FunctionType I HypersensitivityBaker's AsthmaBinding CapacityDot Immunobinding AssayGlycosylated AntigensIge-mediated Allergen IdentificationIge-mediated Food AllergyIge-mediated MechanismsMolecular Basis Of Allergenicity
A 16 kDa protein, designated CM16*, which strongly binds IgE from baker's-asthma patients has been identified as a glycosylated form of the previously reported WTAI-CM16, which is a subunit of the wheat tetrameric alpha-amylase inhibitor. A glycosylated form (CMb*) of BTAI-CMb, the equivalent inhibitor subunit from barley, has been also found to have significantly enhanced IgE-binding capacity. In all, 14 purified members of the alpha-amylase/trypsin-inhibitor family showed very different IgE-binding capacities when tested by a dot-blot assay. The glycosylated components CM16*, CMb* and the previously described non-glycosylated 14.5 kDa allergen from barley (renamed BMAI-1) were found to be the strongest allergens.
20
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
Haider Raza, Annie John, Abderrahim Nemmar · Cellular Physiology and Biochemistry · 2013 · 47.3K citations · Full text
Measurement of protein using bicinchoninic acid
Pam Smith, Randall I. Krohn, Greg T. Hermanson et al. · Analytical Biochemistry · 1985 · 18.4K citations