Tryptophan hydroxylase: Purification by affinity chromatography on calmodulin-Sepharose

Carrol D'Sa, Robert Arthur, Ian Jennings, Richard G.H. Cotton, Donald M. Kuhn

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Abstract

Tryptophan hydroxylase (EC 1.14.16.4; L-tryptophan, tetrahydropteridine:oxygen oxidoreductase (5-hydroxylating)) from rat mesencephalic tegmentum has been purified by sequential chromatography on Blue-Sepharose, DE-52, and calmodulin-Sepharose. The hydroxylase is excluded from Blue-Sepharose and is eluted from DE-52 with a step-wise NaCl gradient. Tryptophan hydroxylase binds to calmodulin-Sepharose in the presence of calcium and is eluted with either EGTA or calmodulin itself, but not with tryptophan. The purification scheme is rapid (5-6 h) and yields an enzyme with a specific activity of 225 nmol 5-HTP/mg min, representing a 400-fold purification with 7% recovery. The tryptophan hydroxylase preparation was judged to be > 95% pure using the present isolation procedure.

Original languageEnglish
Pages (from-to)149-153
Number of pages5
JournalJournal of Neuroscience Methods
Volume69
Issue number2
DOIs
Publication statusPublished - 1 Nov 1996
Externally publishedYes

Keywords

  • Affinity chromatography
  • Brain
  • Calmodulin
  • Protein purification
  • Tryptophan hydroxylase

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