Characterization of fetal serum 5′-nucleotide phosphodiesterase:: A novel function as a platelet aggregation inhibitor in fetal circulation

被引：35

作者：

Sakura, H ^{[1
]}

Nagashima, S ^{[1
]}

Nakashima, A ^{[1
]}

Maeda, M ^{[1
]}

机构：

[1] Hamamatsu Med Ctr, Dept Obstet & Gynecol, Hamamatsu, Shizuoka 4328580, Japan

来源：

THROMBOSIS RESEARCH | 1998年 / 91卷 / 02期

关键词：

5'-nucleotide phosphodiesterase; ADP; platelet aggregation;

D O I：

10.1016/S0049-3848(98)00073-5

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

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. (C) 1998 Elsevier Science Ltd.

引用

页码：83 / 89

页数：7

共 45 条

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