Abstract
The partial amino acid sequence of a low molecular weight folate binding protein from human milk has been determined from N-terminal sequencing of the native protein and isolated cyanogen bromide fragments. A molecular weight of approximately 30,000 is estimated on the basis of amino acid composition and sequence homology with the low-molecular weight folate binder isolated from cow's milk. Preliminary studies with a large molecular weight folate binding protein have shown that the N-terminal amino acid sequence is identical with that of the low molecular binder.
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