Composite Organization of the Cobalamin Binding and Cubilin Recognition Sites of Intrinsic Factor
Copyright policy )Composite Organization of the Cobalamin Binding and Cubilin Recognition Sites of Intrinsic Factor
Intrinsic factor (IF(50)) is a cobalamin (Cbl)-transporting protein of 50 kDa, which can be cleaved into two fragments: the 30 kDa N-terminal peptide IF(30) and the 20 kDa C-terminal glycopeptide IF(20). Experiments on binding of Cbl to IF(30), IF(20), and IF(50) revealed comparable association rate constants (k(+)(Cbl) = 4 x 10(6), 14 x 10(6), and 26 x 10(6) M(-1) s(-1), respectively), but the equilibrium dissociation constants were essentially different (K(Cbl) = 200 microM, 0.2 microM, and
- Aarhus University Hospital Denmark
- Aarhus University Denmark
Intrinsic Factor, Binding Sites, Receptors, Cell Surface, Surface Plasmon Resonance, Peptide Fragments, Recombinant Proteins, Kinetics, Vitamin B 12, Spectrometry, Fluorescence, Humans, Cobalt Radioisotopes, Protein Processing, Post-Translational, Protein Binding
Intrinsic Factor, Binding Sites, Receptors, Cell Surface, Surface Plasmon Resonance, Peptide Fragments, Recombinant Proteins, Kinetics, Vitamin B 12, Spectrometry, Fluorescence, Humans, Cobalt Radioisotopes, Protein Processing, Post-Translational, Protein Binding
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