Abstract
Human jejunal fluid contains a protein which has a molecular radius of 3.37 nm, an M r of 60 600 and a mena p I of 3.35 and binds a cobalamin with a K of 0.1 · 10 9 l/mol. This protein also couples cobalaminanalogues lacking the nucleotide moiety, cross-reacts with R-type proteins and is resistant to proteolysis in the intestine. These findings refute the hypothesis that cobalamin-analogue binders are present and effectively inhibit the bacterial uptake of analogues in the intestine.
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