Binding capacities of various analogues of S-adenosyl-L-homocysteine to protein methyltransferase II from human erythrocytes |
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Authors: | L Gillet Y Looze M Deconinck J Léonis |
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Institution: | (1) Laboratoire de Chimie Générale I, Faculté des Sciences, Université libre de Bruxelles, 50, Avenue F. D. Roosevelt, B-1050 Bruxelles, Belgium |
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Abstract: | Summary A series of analogues of S-adenosyl-L-homocysteine, modified mainly in the amino acid portion of the molecule, have been synthesized. All were found to be competitive inhibitors of protein methyltransferase II from human erythrocytes. S-adenosyl-L-homocysteine remains however by far the most effective inhibitor of the methylase.Acknowledgments. This work was supported by a grant of the Fonds National Belge de la Recherche Scientifique and by a grant of the Fonds Emile Defay. |
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