LIGAND-BINDING STUDIES WITH A 23-KDA PROTEIN PURIFIED FROM BOVINE BRAIN CYTOSOL
LIGAND-BINDING STUDIES WITH A 23-KDA PROTEIN PURIFIED FROM BOVINE BRAIN CYTOSOL
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DOI：
10.1016/0167-4838(86)90128-7
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发表时间：
1986-05-12
期刊：
影响因子：
--
通讯作者：
JOLLES, P
中科院分区：
文献类型：
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作者：
BERNIER, I;TRESCA, JP;JOLLES, P
使用从牛脑细胞质中纯化的碱性 23 kDa 蛋白质进行配体结合研究。通过平衡透析实验溴磺酞、硫酸脱氢表雄酮和雌二醇-17.β。被证明以 1.cntdot 的关联常数与蛋白质结合。 106, 1 .cnt点。 104 和 1 .cntdot。分别为 103 升/摩尔。吲哚菁绿、伊文思蓝和玫瑰红没有结合。该蛋白被进一步鉴定为磷脂酰乙醇胺结合蛋白，而磷脂转移测定结果呈阴性。迄今为止研究的 23 kDa 胞质蛋白的结合特征，以及先前证明的与其他已知胞质蛋白的序列同源性，表明它参与脂质代谢。
Ligand-binding studies were performed with a basic 23 kDa protein purified from bovine brain cytosol. By equilibrium dialysis experiments bromosulfophthalein, dehydroepiandrosterone sulfate and oestradiol-17.beta. were demonstrated to bind to the protein with association constants of 1 .cntdot. 106, 1 .cntdot. 104 and 1 .cntdot. 103 l/mol, respectively. Indocyanine green, Evans blue and Rose Bengal were not bound. The protein was further characterized as a phosphatidylethanolamine-binding protein, while phospholipid transfer assays proved negative. The so far investigated binding characteristics of the 23 kDa cytosolic protein, together with previously demonstrated sequence homologies with other known cytosolic proteins, suggest its involvement in lipid metabolism.