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Characterization of fetal serum 5'-nucleotide phosphodiesterase : a novel function as a platelet aggregation inhibitor in fetal circulation
Bibliographic Information
- Other Title
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- Characterization of Fetal Serum 5′-Nucleotide Phosphodiesterase
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Description
The study was performed to indicate the ADPase activity of 5'-nucleotide phosphodiesterase (PDEase) from human umbilical cord blood serum and demonstrates the effect of this enzyme on ADP-induced platelet aggregation. The PDEase was purified by using p-nitrophenyl-5'-TMP as a substrate. The PDEase had a molecular weight of 128,000 daltons, and activity of 103 nmol/min/mg protein. The PDEase activity was inhibited by 5'-AMP, ADP, ATP. But 2'-AMP, 3'-AMP, 3':5' cAMP, and adenosine had no inhibiting effects. Kinetic analysis indicated that ADP was a competitive inhibitor with a Ki value of 4.05x10(-5) M. The enzyme was markedly inhibited by 1 mM EDTA. The ADPase activity of the PDEase was 7.79 nmol/min/mg protein. The hydrolized products of ADP by the PDE ase were AMP and phosphoric acid. The platelet aggregation by ADP was inhibited by the addition of the PDEase in the platelet-rich plasma.
Journal
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- Thromb. Res.
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Thromb. Res. 91 83-89, 1998
Elsevier BV
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Keywords
Details 詳細情報について
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- CRID
- 1573105976013775104
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- NII Article ID
- 30006323570
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- NII Book ID
- AA00863148
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- ISSN
- 00493848
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- PubMed
- 9722024
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- Data Source
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- CiNii Articles
- OpenAIRE