DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, JS | ko |
dc.contributor.author | Kim, WY | ko |
dc.contributor.author | Rho, HW | ko |
dc.contributor.author | Park, JW | ko |
dc.contributor.author | Park, BH | ko |
dc.contributor.author | Han, MK | ko |
dc.contributor.author | Kim, UH | ko |
dc.contributor.author | Kim, HR | ko |
dc.date.accessioned | 2024-03-22T06:04:38Z | - |
dc.date.available | 2024-03-22T06:04:38Z | - |
dc.date.created | 2024-03-21 | - |
dc.date.created | 2024-03-21 | - |
dc.date.created | 2024-03-21 | - |
dc.date.issued | 1998-05 | - |
dc.identifier.citation | INTERNATIONAL JOURNAL OF BIOCHEMISTRY CELL BIOLOGY, v.30, no.5, pp.629 - 638 | - |
dc.identifier.issn | 1357-2725 | - |
dc.identifier.uri | http://hdl.handle.net/10203/318770 | - |
dc.description.abstract | Free ADP-ribose is a turnover product of NAD(+), protein-bound polymeric and monomeric ADP-ribose, and cyclic ADP-ribose. But little is known about the specific cellular roles or metabolism of free ADP-ribose. ADP-ribose pyrophosphatase (EC 3.6.1.13), which hydrolyzes ADP-ribose into AMP and ribose-5'-phosphate, was purified from human erythrocytes. Purification was achieved to homogeneity by successive chromatographic steps, resulting in a final purification of 75,790-fold from the hemolysate. The purified enzyme showed a single band with the molecular weight of 34 kDa on SDS-PAGE both in the presence and absence of 2-mercaptoethanol. The molecular weight of the native enzyme calculated by gel filtration was 68 kDa, indicating that the active enzyme is a dimer of identical subunits. The enzyme requiring Mg2+ showed highest activity toward ADP-ribose, and about 40-70% activities with IDP-ribose, ADP-mannose and GDP-mannose. The enzyme showed a K-m of 169 +/- 11 mu M for ADP-ribose, broad pH optimum around pH 9.5, and pi of 5.1. ADP was a potent noncompetitive inhibitor with a K-i of 16 +/- 1.2 mu M. These results suggest that our enzyme is unique, and different from the other ADP-ribose pyrophosphatases reported. ADP-ribose pyrophosphatase may play an important role in the regulation of intracellular steady-state of free ADP-ribose. (C) 1998 Elsevier Science Ltd. All rights reserved. | - |
dc.language | English | - |
dc.publisher | PERGAMON-ELSEVIER SCIENCE LTD | - |
dc.title | Purification and characterization of adenosine diphosphate ribose pyrophosphatase from human erythrocytes | - |
dc.type | Article | - |
dc.identifier.wosid | 000074703700010 | - |
dc.identifier.scopusid | 2-s2.0-0031866405 | - |
dc.type.rims | ART | - |
dc.citation.volume | 30 | - |
dc.citation.issue | 5 | - |
dc.citation.beginningpage | 629 | - |
dc.citation.endingpage | 638 | - |
dc.citation.publicationname | INTERNATIONAL JOURNAL OF BIOCHEMISTRY CELL BIOLOGY | - |
dc.identifier.doi | 10.1016/S1357-2725(97)00142-8 | - |
dc.contributor.localauthor | Park, BH | - |
dc.contributor.nonIdAuthor | Kim, JS | - |
dc.contributor.nonIdAuthor | Kim, WY | - |
dc.contributor.nonIdAuthor | Rho, HW | - |
dc.contributor.nonIdAuthor | Park, JW | - |
dc.contributor.nonIdAuthor | Han, MK | - |
dc.contributor.nonIdAuthor | Kim, UH | - |
dc.contributor.nonIdAuthor | Kim, HR | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | ADP-ribose | - |
dc.subject.keywordAuthor | ADP-ribose pyrophosphatase | - |
dc.subject.keywordAuthor | human | - |
dc.subject.keywordAuthor | erythrocyte | - |
dc.subject.keywordPlus | FREE ADP-RIBOSE | - |
dc.subject.keywordPlus | RAT-LIVER | - |
dc.subject.keywordPlus | NUCLEOTIDE PYROPHOSPHATASE | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | DINUCLEOSIDETRIPHOSPHATASE | - |
dc.subject.keywordPlus | METABOLITES | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | NAD | - |
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