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斑纹电鳐电器官中突触体ATP二磷酸水解酶的特性研究

Characterization of a synaptosomal ATP diphosphohydrolase from the electric organ of Torpedo marmorata.

作者信息

Sarkis J J, Salto C

机构信息

Departamento de Bioquimica, Universidade Federal do Rio Grande do Sul Porto Alegre, RS, Brasil.

出版信息

Brain Res Bull. 1991 Jun;26(6):871-6. doi: 10.1016/0361-9230(91)90251-e.

Abstract

A true ecto-apyrase (ATP diphosphohydrolase, EC 3.6.1.5) enzyme was found in the synaptosomal fraction from the electric organ of the electric ray Torpedo marmorata. The activity could not be attributed to the combined action of different enzymes. The pH requirement and calcium dependence were the same for hydrolysis of both substrates ADP and ATP. The enzyme had an apparent Km value of 117 microM for ATP and of 123 microM for ADP. The involvement of nonspecific phosphatases in the hydrolysis of both substrates was excluded. The enzyme hydrolyses almost equally well different nucleoside di- and triphosphates. ATP and ADP hydrolysis was not inhibited by seven ATPase inhibitors, i.e., sodium azide, dinitrophenol, ruthenium red, oligomycin, ouabain, sodium orthovanadate and lanthanum.

摘要

在电鳐(Torpedo marmorata)电器官的突触体部分发现了一种真正的胞外腺苷三磷酸双磷酸酶(ATP二磷酸水解酶,EC 3.6.1.5)。该活性不能归因于不同酶的联合作用。对于底物ADP和ATP的水解,pH要求和对钙的依赖性是相同的。该酶对ATP的表观Km值为117微摩尔,对ADP的表观Km值为123微摩尔。排除了非特异性磷酸酶参与两种底物水解的可能性。该酶对不同的核苷二磷酸和三磷酸的水解效果几乎相同。七种ATP酶抑制剂,即叠氮化钠、二硝基苯酚、钌红、寡霉素、哇巴因、原钒酸钠和镧,均不抑制ATP和ADP的水解。

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