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Potential inhibitors of S-adenosylmethionine-dependent methyltransferases. 1. Modification of the amino acid portion of S-adenosylhomocysteine

โœ Scribed by Borchardt, Ronald T.; Wu, Yih Shiong


Book ID
126205924
Publisher
American Chemical Society
Year
1974
Tongue
English
Weight
890 KB
Volume
17
Category
Article
ISSN
0022-2623

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Affinity chromatography of an S-adenosyl
โœ J.P.G. Mack; M.B. Slaytor ๐Ÿ“‚ Article ๐Ÿ“… 1978 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 579 KB

In the cases that have been studied so far, S-adenosylhomocysteine (SAH) is a powerful inhibitor of S-adenosylmethionine (SAM) binding to SAM-dependent methyltransferases. We deduced, from the available data on the binding of SAM and SAH analogues to SAM dependent methyltransferases, that linkage of