Allergenic activities of major component proteins of soybean 11S-, 7S- and 2S-globulins were examined by the radioallergosorbent test (RAST) and by RAST inhibition experiments with the sera from soybean-sensitive patients. The reactivity with specific IgE antibody was found in all fractions. There was considerable cross-reactivity among three fractions, and 2S-globulin had the highest allergen potency to inhibit the RAST against 11S-, 7S- and 2S-globulin. When the fractions were heat-treated at 80, 100 and 120 °C for 30 min, the RAST reactivity of 2S-globulin heated at 80 °C for 30 min was slightly enhanced, while that of others was reduced to 39–75% of that of the native globulin. IgE antibody could be produced in BALB/c mice only with one of the three fractions, i. e. 2S-globulin, and the produced IgE antibody lacked reactivity with 11S- and 7S-globulin.
Epidermal growth factor (EGF) in human milk, cow's milk and 10 different milk formulas was measured by radioreceptor assay (RRA) using human placental membrane as an EGF receptor. The raw and pasteurized cow's milk contained 324.2 ng/ml and 155.0 ng/ml of RRA-EGF, respectively. These values were almost the same as that found in human milk, when the concentration was expressed as the proportion of protein contents in the samples. On the other hand, no trace of RRA-EGF was detected in 9 different milk formulas, and only one contained a very small amount of it.
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