The stimulation of partially purified bovine caudate tyrosine hydroxylase by phosphatidyl-L-serine

Thomas Lloyd, S. Kaufman

Research output: Contribution to journalArticle

89 Citations (Scopus)

Abstract

A new procedure has been developed for the purification of tyrosine hydroxylase from bovine caudate nucleus. This procedure yields a soluble and stable enzyme which has been purified 50-fold from an acetone powder extract. The enzyme is stimulated greater than 3-fold by phosphatidyl-L-serine and other polyanions which lower the Km of the enzyme for the pterin cofactor. Substrate inhibition and an ability to readily hydroxylate phenylalanine in the presence of tetrahydrobiopterin have also been observed with this preparation.

Original languageEnglish (US)
Pages (from-to)1262-1269
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume59
Issue number4
DOIs
StatePublished - Aug 19 1974

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Phosphatidylserines
Tyrosine 3-Monooxygenase
Serine
Pterins
Caudate Nucleus
Coenzymes
Enzymes
Acetone
Phenylalanine
Powders
Purification
Substrates
sapropterin
polyanions

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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The stimulation of partially purified bovine caudate tyrosine hydroxylase by phosphatidyl-L-serine. / Lloyd, Thomas; Kaufman, S.

In: Biochemical and Biophysical Research Communications, Vol. 59, No. 4, 19.08.1974, p. 1262-1269.

Research output: Contribution to journalArticle

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AU - Kaufman, S.

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