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
Mesh Terms:
Binding Sites, Cobalt Radioisotopes, Humans, Intrinsic Factor, Kinetics, Peptide Fragments, Protein Binding, Protein Processing, Post-Translational, Receptors, Cell Surface, Recombinant Proteins, Spectrometry, Fluorescence, Surface Plasmon Resonance, Vitamin B 12
Binding Sites, Cobalt Radioisotopes, Humans, Intrinsic Factor, Kinetics, Peptide Fragments, Protein Binding, Protein Processing, Post-Translational, Receptors, Cell Surface, Recombinant Proteins, Spectrometry, Fluorescence, Surface Plasmon Resonance, Vitamin B 12
Biochemistry
Date: Mar. 08, 2005
PubMed ID: 15736970
View in: Pubmed Google Scholar
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