SUMMARY: The extracellular cobalamin (Cbl) binding protein from was purified and some properties of the protein were studied for the elucidation of its physiological role. The protein was purified about 20-fold with a yield of 15% and was homogeneous on PAGE. SDS-PAGE indicated that the protein had a single type of polypeptide of 56000. The protein could bind some Cbl analogues with different β-coordination moieties, over a wide range of pH values from 4.0 to 9.0, and the value for cyanocobalamin was 1.1 n. The extracellular Cbl binding protein was located on the cell surface of , probably bound in the muciferous layer.


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