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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Glutamate decarboxylase solubilized from the rat cerebral cortex by two different concentrations of Triton X-100: effects of glutamate analogues and analysis by SDS-PAGE/western blotting using GAD6 and K2 antibodies.
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Glutamate decarboxylase solubilized from the rat cerebral cortex by two different concentrations of Triton X-100: effects of glutamate analogues and analysis by SDS-PAGE/western blotting using GAD6 and K2 antibodies.

机译：谷氨酸脱羧酶可通过两种不同浓度的Triton X-100从大鼠大脑皮层中溶解：谷氨酸类似物的作用以及使用GAD6和K2抗体的SDS-PAGE / western印迹分析。

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摘要

Analysis of two preparations (containing 0.1% and 0.5% Triton X-100) of glutamate decarboxylase (GAD) by Western blotting using GAD6 and K2 antibodies specifically recognizing two GAD isoenzymes, GAD65 and GAD67, respectively, indicated that the higher concentration of Triton X-100 at best only moderately favoured solubilization of GAD67. Several glutamate analogues were found to be either equally potent or equally inactive as inhibitors of glutamate decarboxylase activities in the two preparations. Among typical ligands for glutamate receptors and transporters, only quinolinic and L-cysteine sulphinic acids were weak inhibitors of GAD. Kainate, alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionate (AMPA), 3-((RS)-carboxypiperazin-4-yl)-propyl-1-phosphonic acid (CPP), L-threo-3-hydroxy-aspartate, L-trans-pyrrolidine-2,4-dicarboxylate, dihydrokainate, kynurenic acid and N-methyl-D-aspartate were inactive. Even though the activity of glutamate decarboxylase in homogenates of rat cerebral cortex is higherat 0.5% than at 0.1% Triton X-100, structural requirements of the enzyme active site appear to be independent of Triton X-100 concentration. Furthermore, since the less soluble component of the enzyme activity contains about the same ratio of GAD65 to GAD67 as the more soluble one, it does not seem that the fractionation with Triton X-100 can be easily used to separate the two isoenzymes from each other.
机译：使用特异识别两种GAD同工酶GAD65和GAD67的GAD6和K2抗体通过蛋白质印迹分析两种谷氨酸脱羧酶（GAD）制剂（分别含有0.1％和0.5％Triton X-100）表明，较高的Triton X浓度-100最多仅适度偏向于GAD67的溶解。在这两种制剂中，发现几种谷氨酸类似物与谷氨酸脱羧酶活性的抑制剂同等效力或无活性。在谷氨酸受体和转运蛋白的典型配体中，只有喹啉酸和L-半胱氨酸亚磺酸是GAD的弱抑制剂。海藻酸酯，α-氨基-3-羟基-5-甲基-4-异唑-丙酸酯（AMPA），3-（（RS）-羧基哌嗪-4-基）-丙基-1-膦酸（CPP），L-苏氨酸-3-羟基天冬氨酸盐，L-反式吡咯烷-2,4-二羧酸盐，二氢海藻酸盐，犬尿酸和N-甲基-D-天冬氨酸盐是无活性的。尽管大鼠大脑皮层匀浆中的谷氨酸脱羧酶活性比0.1％Triton X-100高0.5％，但酶活性位点的结构要求似乎与Triton X-100浓度无关。此外，由于酶活性的溶解度较低的组分所含的GAD65与GAD67的比例与溶解度较高的组分的比例大致相同，因此似乎不容易将Triton X-100的馏分用于将两种同工酶彼此分离。

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