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Research Article
Glycine N-methyltransferase is a folate binding protein of rat liver cytosol
R J Cook and C Wagner

Abstract
A comparison of the amino acid compositions of one of the folate-binding proteins of rat liver cytosol, folate-binding protein-cytosol II, and that of glycine N-methyltransferase (S-adenosyl-L-methionine:glycine methyltransferase, EC 2.1.1.20) from the same source indicated a great deal of structural homology between the two proteins. Antiserum prepared against the purified folate-binding protein almost completely inactivated the enzyme activity in crude liver cytosol. Purification of glycine N-methyltransferase resulted in the separation of two enzyme species, one that contained bound folate and one that did not. Each species was homogeneous, as judged by NaDodSO4/polyacrylamide gel electrophoresis, and they migrated identically.
Glycine N-methyltransferase is a folate binding protein of rat liver cytosol
R J Cook, C Wagner
Proceedings of the National Academy of Sciences Jun 1984, 81 (12) 3631-3634; DOI: 10.1073/pnas.81.12.3631
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