The Immunoreactive Protein was Produced During Absorption of Glycinin or its Hydrolysate in IPEC-J2

The allergens absorbed in immunoreactive form by the gut epithelium might induce the occurrence of allergy. The purpose of this study was to investigate the absorption and intracellular accumulation of the intact or hydrolyzed glycinin in the porcine intestinal epithelial cells (IPEC-J2). The IPEC-J2 cells were incubated by 0, 0.25, 0.5 and 1.0 mg/mL glycinin or its hydrolysate for 2, 4, 8 or 12 h. The amounts of immunoreactive glycinin were measured by enzyme-linked immunosorbent assay. The intact and hydrolyzed glycinin fragments of epithelial absorption were identified by immunoblotting and mass spectrometry (MS). We found that glycinin or its hydrolysate is expensively absorbed with the increase of dose and time. The 35 kD or 22 kD protein with glycinin-specific epitopes was detected in the intracellular extracts and basolateral solutions. The results indicate that the glycinin or its hydrolysate could be absorbed; meanwhile, the 35kD or 22kD protein was correspondingly produced during absorption.