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首页> 外文期刊>Molecular and Cellular Biology >Ras GTPase-activating protein physically associates with mitogenically active phospholipids.
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Ras GTPase-activating protein physically associates with mitogenically active phospholipids.

机译：Ras GTPase激活蛋白与促丝裂活性磷脂物理缔合。

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摘要

The physical interaction between GTPase-activating protein (GAP) and lipids has been characterized by two separate analyses. First, bacterially synthesized GAP molecules were found to associate with detergent-mixed micelles containing arachidonic but not with those containing arachidic acid. This association was detected by a faster elution time during molecular exclusion chromatography. Second, GAP molecules within a crude cellular lysate were specifically retained by a column on which certain lipids had been immobilized. The lipids able to retain GAP on such columns were identical to those which were shown previously to be most active in blocking GAP activity. The association between lipids and GAP was dependent upon magnesium ions. Lipids unable to inhibit GAP activity were also unable to physically associate with GAP. The tight association of GAP with these lipids was predicted by and helps to rationalize their ability to inhibit GAP activity.
机译：GTPase激活蛋白（GAP）与脂质之间的物理相互作用已通过两次单独的分析进行了表征。首先，发现细菌合成的GAP分子与含有花生四烯酸的去污剂混合胶束缔合，而与含有花生四烯酸的胶束不缔合。通过分子排阻色谱法中更快的洗脱时间可以检测到这种关联。其次，粗细胞裂解液中的GAP分子被固定了某些脂质的色谱柱特异性保留。能够在此类色谱柱上保留GAP的脂质与先前显示出在阻断GAP活性方面最活跃的脂质相同。脂质和GAP之间的关联取决于镁离子。无法抑制GAP活性的脂质也不能与GAP物理缔合。这些脂质预测了GAP与这些脂质的紧密结合，并有助于合理化其抑制GAP活性的能力。

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