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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Del Rio M J, Velez-Pardo C, Ebinger G, Vauquelin G

Department of Protein Chemistry, Institute of Molecular Biology, Free University Brussels (VUB), Belgium.

Gen Pharmacol. 1995 Dec;26(8):1633-41. doi: 10.1016/0306-3623(95)00063-1.

Serotonin binding proteins (SBP, 45 and 56 kDa) were initially believed to store, transport and/or protect serotonin in serotonergic neurons and, later, to play a catecholamine "housekeeping" function as well. 2. Monoamines do not form coordination bonds with a preformed iron-SBP complex, as initially believed. Instead, metals oxidise the monoamines either directly (manganese, copper) or via oxygen free radical formation (iron) and the oxidation products bind covalently to SBP. 3. SBP are not involved in the housekeeping of monoamines and actin is likely to represent the 45 kDa form. 4. SBP are targets of catecholamine and serotonin-related neurotoxins and monoamine-SBP binding could represent an in vitro model for neurotoxicity.

血清素结合蛋白（SBP，45 kDa和56 kDa）最初被认为在血清素能神经元中储存、运输和/或保护血清素，后来也被认为具有儿茶酚胺“管家”功能。2. 单胺并不像最初认为的那样与预先形成的铁-SBP复合物形成配位键。相反，金属直接（锰、铜）或通过形成氧自由基（铁）氧化单胺，氧化产物与SBP共价结合。3. SBP不参与单胺的管家功能，肌动蛋白可能代表45 kDa的形式。4. SBP是儿茶酚胺和血清素相关神经毒素的靶点，单胺-SBP结合可能代表神经毒性的体外模型。

Del Rio M J, Velez-Pardo C, Ebinger G, Vauquelin G

Department of Protein Chemistry, Institute of Molecular Biology, Free University Brussels (VUB), Belgium.

Gen Pharmacol. 1995 Dec;26(8):1633-41. doi: 10.1016/0306-3623(95)00063-1.

Serotonin binding proteins (SBP, 45 and 56 kDa) were initially believed to store, transport and/or protect serotonin in serotonergic neurons and, later, to play a catecholamine "housekeeping" function as well. 2. Monoamines do not form coordination bonds with a preformed iron-SBP complex, as initially believed. Instead, metals oxidise the monoamines either directly (manganese, copper) or via oxygen free radical formation (iron) and the oxidation products bind covalently to SBP. 3. SBP are not involved in the housekeeping of monoamines and actin is likely to represent the 45 kDa form. 4. SBP are targets of catecholamine and serotonin-related neurotoxins and monoamine-SBP binding could represent an in vitro model for neurotoxicity.

血清素结合蛋白（SBP，45 kDa和56 kDa）最初被认为在血清素能神经元中储存、运输和/或保护血清素，后来也被认为具有儿茶酚胺“管家”功能。2. 单胺并不像最初认为的那样与预先形成的铁-SBP复合物形成配位键。相反，金属直接（锰、铜）或通过形成氧自由基（铁）氧化单胺，氧化产物与SBP共价结合。3. SBP不参与单胺的管家功能，肌动蛋白可能代表45 kDa的形式。4. SBP是儿茶酚胺和血清素相关神经毒素的靶点，单胺-SBP结合可能代表神经毒性的体外模型。