Purification of rat liver S adenosyl L methionine decarboxylase

Research output: Contribution to journalArticle

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)581-583
Number of pages3
JournalBiochemical Journal
Volume141
Issue number2
DOIs
StatePublished - Jan 1 1974

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S-Adenosylmethionine
Liver
Purification
Rats
Spermidine Synthase
Mitoguazone
Liver Extracts
Enzyme Inhibitors
Enzymes
Chromatography
Sepharose
methionine decarboxylase

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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Purification of rat liver S adenosyl L methionine decarboxylase. / Pegg, A. E.

In: Biochemical Journal, Vol. 141, No. 2, 01.01.1974, p. 581-583.

Research output: Contribution to journalArticle

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