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

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

Research output: Contribution to journalArticle

29 Citations (Scopus)

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
StatePublished - Jan 1 1994

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Tryptophan Hydroxylase
Cyclic AMP-Dependent Protein Kinases
Rabbits
Substrates
Enzymes
Phosphorylation
Enzyme activity
Catalytic Domain
Bacteria
Peptide Hydrolases
Complementary DNA
Clone Cells
Genes
Adenosine Triphosphate
Gene Expression
Proteins
Experiments

All Science Journal Classification (ASJC) codes

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

Cite this

Vrana, Kent ; Rucker, Paul J. ; Kumer, Sean C. / Recombinant rabbit tryptophan hydroxylase is a substrate for cAMP-dependent protein kinase. In: Life Sciences. 1994 ; Vol. 55, No. 13. pp. 1045-1052.
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Recombinant rabbit tryptophan hydroxylase is a substrate for cAMP-dependent protein kinase. / Vrana, Kent; Rucker, Paul J.; Kumer, Sean C.

In: Life Sciences, Vol. 55, No. 13, 01.01.1994, p. 1045-1052.

Research output: Contribution to journalArticle

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