A nucleoside diphosphokinase from liver mitochondria which catalyzes an [ 32P] ADP-ATP exchange reaction

A nucleoside diphosphokinase has been purified 50- to 100-fold from aqueous extracts of porcine-liver mitochondria. The enzyme can catalyze transphosphorylation reactions between a number of nucleoside di- and triphosphates, e.g., an exchange between [ 32P] ADP and ATP, and accounts for a substantia...

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Published inBiochimica et biophysica acta Vol. 61; no. 5; pp. 736 - 740
Main Authors Chiga, M., Plaut, G.W.E.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 26.11.1962
Subjects
Adenine Nucleotides
Adenosine Diphosphate
Adenosine Triphosphate
Liver
Mitochondria
Mitochondria, Liver
Nucleoside-Diphosphate Kinase
Phosphotransferases
p-hydroxymercuribenzoate
p-OHMB
PHOSPHOTRANSFERASES
ADENINE NUCLEOTIDES
LIVER
MITOCHONDRIA
ADENOSINE TRIPHOSPHATE
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Summary:A nucleoside diphosphokinase has been purified 50- to 100-fold from aqueous extracts of porcine-liver mitochondria. The enzyme can catalyze transphosphorylation reactions between a number of nucleoside di- and triphosphates, e.g., an exchange between [ 32P] ADP and ATP, and accounts for a substantial portin of the ADP-ATP exchange activity of such extracts. The ADP-ATP exchange is not catalyzed. The reaction is activated by Mg 2+ or Mn 2, and is not inhibited by low concentrations of sulfhydryl-group binding agents.
ISSN:0926-6550
0006-3002
1878-2256
DOI:10.1016/0926-6550(62)90056-7