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.