Porcine colostrum and milk were separated into the acid-soluble fraction (SF) and casein frac-tion (CF) by centrifuge. Trypsin and chymotrypsin inhibitory capacity in porcine colostrum, milk and theircomponents were d...Porcine colostrum and milk were separated into the acid-soluble fraction (SF) and casein frac-tion (CF) by centrifuge. Trypsin and chymotrypsin inhibitory capacity in porcine colostrum, milk and theircomponents were determined by incubating bovine trypsin or chymotrypsin in a medium. The inhibition of in-sulin-like growth factor Ⅰ (IGF-Ⅰ) and epidermal growth factor (EGF) degradation in pig small intestinal con-tents by porcine colostrum was measured by incubating iodinated IGF-Ⅰ or EGF. Degradation of labeled IGF-Ⅰor EGF was determined by monitoring the generation of radioactivity soluble in 30% trichloroacetic acid(TCA). The results showed that porcine colostrum had high levels of trypsin and chymotrypsin inhibitory ac-tivity and increased the stability of IGF-Ⅰ and EGF in pig intestinal contents. The SF was higher in inhibitorypotency than CF. The present study revealed that the protease inhibitors in porcine colostrum, milk-derivedand colostrum-specific, existed mainly in SF.展开更多
Porcine colostrum was separated into the acid soluble fraction (SF) and casein fraction (CF) by acidifying followed by centrifuge. SF was further separated by liquid chromatography and anisotropic membrane filtration....Porcine colostrum was separated into the acid soluble fraction (SF) and casein fraction (CF) by acidifying followed by centrifuge. SF was further separated by liquid chromatography and anisotropic membrane filtration. Capacities of the SF or CF of porcine colostrum, to inhibit trypsin and chymotrypsin activity and to inhibit the epidermal growth factor (EGF) degradation in pig small intestinal contents, were determined under different heat treatments. The study showed that trypsin inhibitors in porcine colostrum survived heat treatments of 100℃ water bath for up to 10 min, but exposure to boiling water bath for 30 min significantly decreased the inhibitory activity. Compared with the trypsin inhibitors, the chymotrypsin inhibitors were more heat sensitive. SF was more heat sensitive than CF. Separation of the SF of porcine colostrum by liquid chromatography and anisotropic membrane filtration revealed that the porcine colostrum protease inhibitors, those had the capacity to inhibit the trypsin chymotrypsin activity and enhanced the stability of EGF in the gastrointestinal(GI) lumen of weaned pigs, existed mainly in SF, milk derived, were a group of heat labile small proteins with molecular weight of 10 00050 000.展开更多
文摘Porcine colostrum and milk were separated into the acid-soluble fraction (SF) and casein frac-tion (CF) by centrifuge. Trypsin and chymotrypsin inhibitory capacity in porcine colostrum, milk and theircomponents were determined by incubating bovine trypsin or chymotrypsin in a medium. The inhibition of in-sulin-like growth factor Ⅰ (IGF-Ⅰ) and epidermal growth factor (EGF) degradation in pig small intestinal con-tents by porcine colostrum was measured by incubating iodinated IGF-Ⅰ or EGF. Degradation of labeled IGF-Ⅰor EGF was determined by monitoring the generation of radioactivity soluble in 30% trichloroacetic acid(TCA). The results showed that porcine colostrum had high levels of trypsin and chymotrypsin inhibitory ac-tivity and increased the stability of IGF-Ⅰ and EGF in pig intestinal contents. The SF was higher in inhibitorypotency than CF. The present study revealed that the protease inhibitors in porcine colostrum, milk-derivedand colostrum-specific, existed mainly in SF.
文摘Porcine colostrum was separated into the acid soluble fraction (SF) and casein fraction (CF) by acidifying followed by centrifuge. SF was further separated by liquid chromatography and anisotropic membrane filtration. Capacities of the SF or CF of porcine colostrum, to inhibit trypsin and chymotrypsin activity and to inhibit the epidermal growth factor (EGF) degradation in pig small intestinal contents, were determined under different heat treatments. The study showed that trypsin inhibitors in porcine colostrum survived heat treatments of 100℃ water bath for up to 10 min, but exposure to boiling water bath for 30 min significantly decreased the inhibitory activity. Compared with the trypsin inhibitors, the chymotrypsin inhibitors were more heat sensitive. SF was more heat sensitive than CF. Separation of the SF of porcine colostrum by liquid chromatography and anisotropic membrane filtration revealed that the porcine colostrum protease inhibitors, those had the capacity to inhibit the trypsin chymotrypsin activity and enhanced the stability of EGF in the gastrointestinal(GI) lumen of weaned pigs, existed mainly in SF, milk derived, were a group of heat labile small proteins with molecular weight of 10 00050 000.
