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首页> 外文期刊>Cell biology international. >Characterization of ATP and ADP hydrolysis activity in rat gastric mucosa.
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Characterization of ATP and ADP hydrolysis activity in rat gastric mucosa.

机译：大鼠胃黏膜中ATP和ADP水解活性的表征。

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摘要

The degradation of nucleotides is catalyzed by the family of enzymes called nucleoside triphosphate diphosphohydrolases (NTPDases). The aim of this work was to demonstrate the presence of NTPDase in the rat gastric mucosa. The enzyme was found to hydrolyze ATP and ADP at an optimum pH of 8.0 in the presence of Mg2+ and Ca2+. The inhibitors ouabain (0.01-1 mM), N-ethylmaleimide (0.01-4 mM), levamisole (0.10-0.2 mM) and Ap5A (0.03 mM) had no effect on NTPDase 1 activity. Sodium azide (0.03-30 mM), at high concentrations (>0.1 mM), caused a parallel hydrolysis inhibition of ATP and ADP. Suramin (50-300 microM) inhibited ATP and ADP hydrolysis at all concentrations tested. Orthovanadate slightly inhibited (15%) Mg2+ and Ca2+ ATP/ADPase at 100 microM. Lanthanum decreased Mg2+ and Ca2+ ATP/ADPase activities. The presence of NTPDase as ecto-enzyme in the gastric mucosa may have an important role in the extracellular metabolism of nucleotides, suggesting that this enzyme plays a role in the control of acid andpepsin secretion, mucus production, and contractility of the stomach.
机译：核苷酸的降解被称为三磷酸核苷二磷酸水解酶（NTPDase）的酶家族催化。这项工作的目的是证明NTPDase在大鼠胃粘膜中的存在。发现该酶在Mg2 +和Ca2 +的存在下，在最适pH值为8.0时水解ATP和ADP。抑制剂哇巴因（0.01-1 mM），N-乙基马来酰亚胺（0.01-4 mM），左旋咪唑（0.10-0.2 mM）和Ap5A（0.03 mM）对NTPDase 1活性无影响。高浓度（> 0.1 mM）的叠氮化钠（0.03-30 mM）引起ATP和ADP的平行水解抑制。苏拉明（50-300 microM）在所有测试浓度下均能抑制ATP和ADP水解。在100 microM时，原钒酸盐轻微抑制（15％）Mg2 +和Ca2 + ATP / ADPase。镧降低了Mg2 +和Ca2 + ATP / ADPase的活性。 NTPDase作为一种外酶在胃粘膜中的存在可能在核苷酸的细胞外代谢中起重要作用，这表明该酶在控制胃酸和胃蛋白酶的分泌，粘液的产生和胃的收缩中起作用。

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