Evidence for the lack of direct phosphorylation of bovine caudate tyrosine hydroxylase following activation by exposure to enzymatic phosphorylating conditions

Tom Lloyd, Seymour Kaufman

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

Highly purified bovine caudate tyrosine hydroxylase can be activated by exposure to enzymatic phosphorylating conditions. This activation is due to both a decrease in the Km for the pterin cofactor and to some increase in Vmax. The Km for the enzyme's substrate, tyrosine, is unchanged by activation. After tyrosine hydroxylase was activated in the presence of [γ-32P]-ATP, no incorporation of 32P into the enzyme was observed by either immunoprecipitation studies or by sucrose gradient studies.

Original languageEnglish (US)
Pages (from-to)907-913
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume66
Issue number3
DOIs
StatePublished - Oct 6 1975

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Phosphorylation
Tyrosine 3-Monooxygenase
Chemical activation
Pterins
Enzymes
Immunoprecipitation
Tyrosine
Sucrose
Adenosine Triphosphate
Substrates

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "Highly purified bovine caudate tyrosine hydroxylase can be activated by exposure to enzymatic phosphorylating conditions. This activation is due to both a decrease in the Km for the pterin cofactor and to some increase in Vmax. The Km for the enzyme's substrate, tyrosine, is unchanged by activation. After tyrosine hydroxylase was activated in the presence of [γ-32P]-ATP, no incorporation of 32P into the enzyme was observed by either immunoprecipitation studies or by sucrose gradient studies.",
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AB - Highly purified bovine caudate tyrosine hydroxylase can be activated by exposure to enzymatic phosphorylating conditions. This activation is due to both a decrease in the Km for the pterin cofactor and to some increase in Vmax. The Km for the enzyme's substrate, tyrosine, is unchanged by activation. After tyrosine hydroxylase was activated in the presence of [γ-32P]-ATP, no incorporation of 32P into the enzyme was observed by either immunoprecipitation studies or by sucrose gradient studies.

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