Solid-phase peptide synthesis and biological activity of bovine thymopoietin II (bTP-II).
Solid-phase peptide synthesis and biological activity of bovine thymopoietin II (bTP-II).
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牛胸腺生成素 II (bTP-II) 的固相肽合成和生物活性。
DOI：
10.1111/j.1399-3011.1994.tb00574.x
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发表时间：
1994
期刊：
影响因子：
--
通讯作者：
Morley,BJ
中科院分区：
文献类型：
--
作者：
Smith,DD;Conlon,JM;Petzel,J;Chen,L;Murphy,RF;Morley,BJ
牛胸腺生成素（bTP）是一种49个氨基酸的多肽，采用梅里菲尔德固相肽合成方法合成。使用阴离子交换色谱和反相HPLC纯化多肽，并通过质谱和全长肽和金黄色葡萄球菌V8蛋白酶消化产物的氨基酸分析进行表征。在几种测定系统中测试合成产物的生物活性。发现合成的bTP诱导来自无胸腺小鼠的T淋巴细胞上Thy 1.2抗原的表达，与先前关于内源性bTP的生物活性的研究一致。在骨骼肌和神经元烟碱乙酰胆碱受体位点的生物活性，如其他人报告的bTP，不能在我们的研究中得到证实。烟碱受体位点缺乏生物活性可能与最近一份报告的结果有关，该报告证明天然bTP制剂中存在眼镜蛇毒素样分子。这些数据表明，合成肽对于评价多肽生物活性的特异性具有重要作用。
Bovine thymopoietin (bTP), a 49 amino acid polypeptide, was synthesized using Merrifield's solid‐phase peptide synthesis methodology. The polypeptide was purified using anion‐exchange chromatography and reversed‐phase HPLC and characterized by mass spectrometry and amino acid analysis of the full‐length peptide and of products derived from digestion withStaphylococcus aureusV8 protease. The biological activity of the synthesized product was tested in several assay systems. Synthetic bTP was found to induce the expression of Thy 1.2 antigen on T‐lymphocytes from athymic mice, in agreement with previous studies on the biological activity of endogenous bTP. Biological activity at skeletal muscle and neuronal nicotinic acetylcholine receptor sites, as reported by others for bTP, could not be confirmed in our studies. The absence of biological activity at nicotinic receptor sites may be related to the results of a recent report demonstrating the presence of a cobratoxin‐like molecule in preparations of natural bTP. These data indicate that synthetic peptides have an important role for the evaluation of the specificity of the biological activity of polypeptides.