Abstract
A single-sited iron-binding fragment of transferrin, prepared by proteolytic cleavage with thermolysin, has been characterized. The fragment, bearing no carbohydrate, must be derived from the N-terminal half of the protein's two homologous domains. The strength of iron-binding at pH 6.7 and 7.4, and the EPR spectroscopic features of its iron and copper complexes, establish it as carying the ‘b’ site of transferrin.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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