Recombinant rabbit tryptophan hydroxylase is a substrate for cAMP-dependent protein kinase

Kent Vrana, Paul J. Rucker, Sean C. Kumer

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Abstract

A full-length cDNA clone for rabbit tryptophan hydroxylase (TPH) was modified and subcloned into a bacterial expression vector. Expression of this gene in the protease-deficient strain of bacteria, BL21[DE3], produced TPH immunoreactive protein which exhibited enzyme activity. Treatment of the recombinant enzyme (in bacterial extracts) with the purified catalytic subunit of the cAMP-dependent protein kinase and [y-32P]-ATP resulted in specific phosphorylation of TPH. This expression system provides a means of generating and purifying large amounts of this important enzyme. Moreover, these experiments establish that TPH will serve as an in vitro substrate for cAMP-dependent protein kinase.

Original languageEnglish (US)
Pages (from-to)1045-1052
Number of pages8
JournalLife Sciences
Volume55
Issue number13
DOIs
Publication statusPublished - Jan 1 1994

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All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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