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.
D000578:Amidines; D002262:Carboxy-Lyases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D002845:Chromatography; D006037:Glyoxal / Q000031:analogs & derivatives; D006835:Hydrazones; D008099:Liver / Q000201:enzymology*; D012436:S-Adenosylmethionine; D013095:Spermidine / Q000096:biosynthesis
D000578:Amidines; D006835:Hydrazones; D006037:Glyoxal; D012436:S-Adenosylmethionine; D002262:Carboxy-Lyases; D013095:Spermidine