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脯氨酸硫代乙内酰脲与硫氰酸铵的形成:迈向可行的C端氨基酸测序程序的进展。

Formation of proline thiohydantoin with ammonium thiocyanate: progress towards a viable C-terminal amino-acid-sequencing procedure.

作者信息

Inglis A S, Duncan M W, Adams P, Tseng A

机构信息

Garvan Institute of Medical Research, St. Vincent's Hospital, Darlinghurst, NSW, Australia.

出版信息

J Biochem Biophys Methods. 1992 Oct;25(2-3):163-71. doi: 10.1016/0165-022x(92)90008-x.

DOI:10.1016/0165-022x(92)90008-x
PMID:1491101
Abstract

Pure amino acid thiohydantoins are required as reference standards for development of C-terminal-sequencing procedures based on thiohydantoin formation of the C-terminal amino acids of peptides and proteins. Proline thiohydantoin was prepared using a straightforward method involving reaction of acetylproline with ammonium thiocyanate. It was characterized by UV spectrophotometry, mass spectrometry and back-hydrolysis to the free amino acid. These data establish unequivocally that the thiocyanate procedure is applicable to proline as well as to the other common amino acids. This work also validates earlier claims that proline thiohydantoin can be prepared by reaction with thiocyanic acid.

摘要

纯氨基酸乙内酰硫脲是基于肽和蛋白质C端氨基酸形成乙内酰硫脲来开发C端测序程序所需的参考标准。脯氨酸乙内酰硫脲是通过一种直接的方法制备的,该方法涉及乙酰脯氨酸与硫氰酸铵的反应。通过紫外分光光度法、质谱法以及水解回游离氨基酸对其进行了表征。这些数据明确证实硫氰酸盐程序适用于脯氨酸以及其他常见氨基酸。这项工作还验证了早期关于脯氨酸乙内酰硫脲可通过与硫氰酸反应制备的说法。

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Formation of proline thiohydantoin with ammonium thiocyanate: progress towards a viable C-terminal amino-acid-sequencing procedure.脯氨酸硫代乙内酰脲与硫氰酸铵的形成:迈向可行的C端氨基酸测序程序的进展。
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Molecules. 2022 Sep 23;27(19):6271. doi: 10.3390/molecules27196271.
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An improved chemical approach toward the C-terminal sequence analysis of proteins containing all natural amino acids.一种改进的化学方法用于对包含所有天然氨基酸的蛋白质进行C端序列分析。
Protein Sci. 1998 Jul;7(7):1593-602. doi: 10.1002/pro.5560070713.
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10th International Conference on Methods in Protein Structure Analysis. September 8-13, 1994, Snowbird, Utah. Short communications and abstracts.
第十届蛋白质结构分析方法国际会议。1994年9月8日至13日,犹他州雪鸟城。简短通讯与摘要。
J Protein Chem. 1994 Jul;13(5):431-543.