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The uptake and transmission of protein by neonatal rat enterocytes.
Author(s) -
Morris B,
Morris R,
Solari R
Publication year - 1981
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.1981.sp013593
Subject(s) - heterologous , transferrin , bovine serum albumin , antibody , receptor , context (archaeology) , chemistry , immunoglobulin g , transferrin receptor , lactoferrin , microbiology and biotechnology , biology , biochemistry , immunology , gene , paleontology
1. Proximal enterocytes transmitted intact immunoglobulin G (IgG) preferentially in the order rat, human, sheep and bovine; the removal from the vascular compartment of these transmitted molecules occurred at about the same rate. 2. Heterologous IgGs are processed similarly to rat IgG: they are either transmitted intact or broken down to less than 1000 mol. wt. fragments. 3. All of the human transferrin removed from the intestine was broken down to less than 1000 mol. wt. fragments, but a small amount of bovine serum albumin (BSA) was transmitted intact. 4. The IgGs and BSA are relatively indigestible molecules whereas human transferrin is relatively digestible. 5. These observations are discussed in the context of receptor‐mediated transmission.