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Fig. 2 | Clinical and Translational Allergy

Fig. 2

From: Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure

Fig. 2

Selected SDS-PAGE and immunoblot samples are shown for both LTPs, Pru p 3 and Fra a 3. A Both proteins are highly resistant to pepsin as judged by SDS-PAGE. In contrast, on immunoblot the intensity of recognition by rabbit IgG clearly decreases at t = 10 and t = 60 min. There is a suggestion that this decrease is more significant for Fra a 3, but it cannot be excluded that this is more a result of properties of the rabbit antiserum than of the proteins. In support of this the G0 band of Pru p 3 is more intense than of Fra a 3. B Both proteins not having been exposed to acidic pH are readily digested by pancreatin. When pre-exposed to low pH, Pru p 3 displays significantly higher resistance to pancreatin than its homologue Fra a 3. C Also when IgE is used for immunoblotting both LTPs display high resistance to pepsin. The higher resistance of Pru p 3 to pancreatin is also observed with IgE

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