The enzymatic synthesis of S-adenosyl-l-[2(n)-3H]homocysteine
β Scribed by R.W. Trewyn; S.J. Kerr
- Publisher
- Elsevier Science
- Year
- 1977
- Tongue
- English
- Weight
- 422 KB
- Volume
- 82
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
A rapid, efficient method is described for the enzymatic conversion of S-adenosyl-L-[2(n)-3H]methionine to S-adenosyl-r-[2(n)-3H]homocysteine. Partially purified glycine N-methyltransferase is used in the reaction which yields 98% conversion. The product is purified using high-pressure liquid chromatography and is concentrated by lyophilization.
S-Adenosyl-L-[2(n)-3H]homocysteine synthesized by this method is an active substrate for S-adenosylhomocysteine @AH) hydrolase. A novel assay procedure for SAH hydrolase is also described, in which unreactedS-adenosyl-L-[2(n)-3H]homocysteine is removed by adsorption to dextran-coated charcoal.
π SIMILAR VOLUMES
S-adenosyl-L-homocysteine (AdoHcy) is an important metabolic product in a variety of processes (1.2). This compound as well as 5'-methylthioadenosine are substrates for AdoHcy nucleosidase. an enzyme required In various prokaryotes cells (3.4.5.6) for the recovery of the enzymatic activity of methyl
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