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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 >Solubilization of (35S)lanthionine ketimine binding sites from bovine brain.
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Solubilization of (35S)lanthionine ketimine binding sites from bovine brain.

机译：从牛脑增溶（35S）羊毛硫氨酸酮亚胺结合位点。

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摘要

Lanthionine ketimine (LK) binding sites were solubilized from bovine brain membranes using 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS) and Triton X-100. 10 mM CHAPS in 0.5 M potassium phosphate, pH 7.0, containing 20% glycerol was selected to solubilize LK binding entities. Some properties of CHAPS-solubilized LK binding sites have been studied. The CHAPS-solubilized preparation appeared to contain a homogenous population of binding sites for [35S]LK. Binding properties indicated that the solubilized binding sites were similar to the membrane-bound sites. [35S]LK specific binding was inhibited by other structurally related ketimines obtaining a similar rank order of inhibition for the soluble and the membrane-bound preparations. The successful solubilization of [35S]LK binding sites is a useful starting point for the purification of this binding protein.
机译：使用3-[（（3-胆酰胺基丙基）二甲基铵基] -1-丙烷磺酸盐（CHAPS）和Triton X-100，从牛脑膜上溶解了羊毛硫氨酸酮亚胺（LK）结合位点。选择含有20％甘油的0.5 M磷酸钾（pH 7.0）中的10 mM CHAPS来溶解LK结合实体。 CHAPS增溶的LK结合位点的一些特性已得到研究。 CHAPS增溶的制剂似乎含有[35S] LK的均一结合位点。结合特性表明，溶解的结合位点与膜结合位点相似。 [35S] LK特异性结合受到其他结构相关的酮亚胺的抑制，从而获得了对可溶性和膜结合制剂的相似抑制等级。 [35S] LK结合位点的成功增溶是纯化该结合蛋白的有用起点。

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