Purification of rat liver S-adenosyl-L-methionine decarboxylase.
The amount of S-adenosyl-l-methionine decarboxylase present in rat liver was enhanced 17-fold by administration of methylglyoxal bis(guanylhydrazone),* a specific inhibitor of the enzyme. The enzyme was purified 1400-fold in 50% yield from such liver extracts by chromatography on columns of the inhibitor bound to Sepharose. The purified enzyme had no spermidine synthetase activity.
14 references, click to expand
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Separation and partial purification of S-adenosylmethionine decarboxylase and spermidine and spermine synthases from rat liver.Biochem Biophys Res Commun. 1972 Jan 31;46(2):341-8 PMID: 5057879
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