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Abstract
Human intrinsic factor purified by labile ligand affinity chromatography was cleaved with cyanogen bromide and fractionated by gel filtration. Four of the fragments were purified and sequenced to a total of eighty-four amino acid residues. Including the N-terminal amino acids this amounts to one third of the total amino acid sequence of human intrinsic factor. One of the fragments contained a tyrosine labelled only on iodination of intrinsic factor devoid of cobalamin.
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Schedule a callMore From: Scandinavian journal of clinical and laboratory investigation
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