Synthesis, purification, and chemical characterization of the amino-terminal 1-34 fragment of bovine parathyroid hormone synthesized by the solid-phase procedure.
Synthesis, purification, and chemical characterization of the amino-terminal 1-34 fragment of bovine parathyroid hormone synthesized by the solid-phase procedure.
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固相程序合成的牛甲状旁腺激素氨基末端 1-34 片段的合成、纯化和化学表征。
DOI：
10.1021/bi00632a002
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发表时间：
1977
期刊：
影响因子：
2.9
通讯作者：
J. Potts
中科院分区：
文献类型：
--
作者：
G. Tregear;J. van Rietschoten;R. Sauer;H. Niall;H. Keutmann;J. Potts
在甲状旁腺激素的结构-活性关系的系统研究过程中通过固相合成制备的肽，在连续纯化后，通过各种分析技术（包括Edman程序的序列分析）进行了严格的纯度分析。本论文对肽纯度的不同测试的效用以及在指导和监测最佳合成策略中使用程序进行了严格的评估。代表牛甲状旁腺激素（bPTH-（1-34））氨基末端34个残基的肽的序列分析显示存在至少30%的污染错误肽，这些肽未被其他分析方法检测到。主要的污染物被确定为肽，其中谷氨酰胺在位置29被删除。使用荧光胺而不是茚三酮来监测偶联反应的重复合成导致制备物缺乏由缺失产生的污染物。这些发现证明了序列分析在评价固相技术合成的肽的纯度中的特殊价值。
Peptides prepared by solid-phase synthesis during a systematic study of structure-activity relations in parathyroid hormone have been subjected, after sequential purifications, to rigorous analysis of purity by a variety of analytical techniques including sequence analysis by the Edman procedure. The present paper undertakes a critical appraisal of the utility of different tests of peptide purity and the use of the procedures in guiding and monitoring optimal synthesis strategies. Sequence analysis of a peptide representing the amino-terminal 34 residues of bovine parathyroid hormone (bPTH-(1-34)) revealed the presence of at least 30% of contaminating error peptides which were undetected by other analytical procedures. The major contaminant was identified as a peptid in which glutamine at position 29 was deleted. A repeat synthesis using fluorescamine rather than ninhydrin to monitor the coupling reaction resulted in a preparation that lacked the contaminant resulting from deletion. These findings demonstrate the particular value of sequence analysis in the evaluation of purity of peptides synthesized by the solid-phase technique.