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- W2065579901 abstract "An increasing body of evidence suggests that human milk proteins may vary in their digestibility within the gastrointestinal tract. Secretory IgA, lactoferrin, and lysozyme have all been detected in substantial quantities in the stool of breast-fed infants and in vitro these proteins possess various degrees of stability at low pH and resistance to hydrolysis by pancreatic proteases. We have evaluated the ontogeny of differential milk protein digestibility in a heterologous system by incubating human milk with luminal fluid flushed from the small intestine of 12-day old suckling and 31-day old weanling rats, followed by analysis of protein profiles by electrophoresis in polyacrylamide gels containing SDS. Luminal fluid from the weanling degraded beta-casein most extensively, followed by lactalbumin, lysozyme, and lactoferrin, respectively. Little or no degradation of immunoglobulin could be detected. By contrast, luminal fluid from suckling rats degraded primarily beta-casein, which it hydrolyzed to a lesser extent than did weanling fluid. Other major milk-proteins were minimally digested. Incubation of luminal fluid with 125I human casein followed by measurement of radioactivity in trichloroacetic acid-soluble material demonstrated that weanling hydrolytic capacity was approximately 25-fold greater than that of the suckling for this substrate. These preliminary findings in a heterologous system suggest that differential luminal digestibility of human milk proteins may occur in the small intestine and that the susceptibility of individual protein species to hydrolysis may vary during postnatal development." @default.
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- W2065579901 date "1987-10-01" @default.
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- W2065579901 title "Luminal digestion of human milk proteins in suckling and weanling rats" @default.
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- W2065579901 doi "https://doi.org/10.1016/s0271-5317(87)80175-6" @default.
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