The specific, submicromolar-Km ADP-ribose pyrophosphatase purified from human placenta is enzymically indistinguishable from recombinant NUDT9 protein, including a selectivity for Mn2+ as activating cation and increase in Km for ADP-ribose, both elicited by H2O2

Biochimica et Biophysica Acta - General Subjects

Volumn 1760, Issue 10, 2006, Pages 1545-1551

  Carloto, António ^a   Costas, María Jesús ^a   Cameselle, José Carlos ^a   McLennan, Alexander G ^b   Ribeiro, João Meireles ^a  

^a UNIVERSITY OF EXTREMADURA   (Spain)

^b UNIVERSITY OF LIVERPOOL   (United Kingdom)

Author keywords

Adenosine diphosphate ribose; Adenosine diphosphate ribose pyrophosphatase; Hydrogen peroxide; Nudix hydrolase; Oxidative stress

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; FLUORIDE; HYDROGEN PEROXIDE; INORGANIC PYROPHOSPHATASE; MANGANESE; NUDT 9 PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; ADP RIBOSE PYROPHOSPHATASE I; ADP-RIBOSE PYROPHOSPHATASE I; DITHIOTHREITOL; MAGNESIUM; NUDT9;

ARTICLE; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SPECIFICITY; HUMAN; HUMAN TISSUE; NITROSATION; OXIDATIVE STRESS; PLACENTA; PRIORITY JOURNAL; ENZYMOLOGY; FEMALE; ISOLATION AND PURIFICATION; KINETICS; METABOLISM;

ADENOSINE DIPHOSPHATE RIBOSE; DITHIOTHREITOL; FEMALE; HUMANS; HYDROGEN PEROXIDE; KINETICS; MAGNESIUM; MANGANESE; PLACENTA; PYROPHOSPHATASES; RECOMBINANT PROTEINS;

EID: 33748904083     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.06.003     Document Type: Article

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