Abstract
Neonatal (NB) rat small intestinal MVM bind more food proteins than adult (AD) controls. To study specificity of this binding, bovine serum albumin (BSA) and concan-avalin A (CON A) were radioiodinated. Trace-labelled protein solutions were used for MVM incubation. Separation of unbound material was accomplished by miniature ultracentrifugation. Quantitatively and qualitatively, CON A binding was much different from BSA binding:
The relation between protein concentration and binding was linear for BSA. For CON A, this relation showed different patterns in AD and NB, indicating saturation. CON A binding was specifically inhibited by unlabelled protein and by mannan, whereas BSA binding was not. Trypsin treatment of MVM caused a marked increase (88%) of BSA binding to AD, but not to NB MVM. Contrary to CON A binding, BSA binding was not affected by neuram-inidase. Binding patterns thus exhibited specificity, saturation, and glycoprotein dependence only for CON A. Unlike lectin binding, BSA binding was nonspecific.
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Stern, M., Gellermann, B. DIFFERENT PATTERNS OF FOOD PROTEIN AND LECTIN BINDING TO NEONATAL AND ADULT MICROVILLUS MEMBRANES (MVM). Pediatr Res 20, 689 (1986). https://doi.org/10.1203/00006450-198607000-00025
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DOI: https://doi.org/10.1203/00006450-198607000-00025