Kim J, Kim K
Biotechnology Research Institute, LUCKY Research Park, Yusung, Dae-jeon, Korea.
Biochem Mol Biol Int. 1995 Apr;35(4):803-11.
A new method for the determination of the modified amino acid structures of peptides containing pyroglutamyl residue in their N-terminal position is reported. The combination of fast atom bombardment (FAB) mass spectrometry and pyroglutamate aminopeptidase digestion provides a convenient and sensitive method for the identification of pyroglutamate. In order to investigate the nature of the amino terminal region of the follow post-translationally modified peptides containing pyroglutamyl residues, Neurotensin, Hypertrehalosaemic neuropeptide, and Luteinizing Hormone Releasing Hormone (LH-RH) were digested with pyroglutamate aminopeptidase and analyzed by FAB mass spectrometry. The method provided direct information about the N-terminal structure. The N-terminal pyroglutamates of these peptides are unequivocally determined at a level of 0.9-2.8 nmol per peptide. Several of the complicated procedures and controversies, which accompany the application of traditional methods, are eliminated. We describe the advantages of the combination procedure of FAB mass spectrometry and pyroglutamate aminopeptidase digestion for modified amino acid determination.
报道了一种用于测定N端含有焦谷氨酰残基的肽的修饰氨基酸结构的新方法。快原子轰击（FAB）质谱法与焦谷氨酸氨肽酶消化相结合，为焦谷氨酸的鉴定提供了一种便捷且灵敏的方法。为了研究以下含有焦谷氨酰残基的翻译后修饰肽的氨基末端区域的性质，用焦谷氨酸氨肽酶消化神经降压素、高海藻糖血神经肽和促黄体激素释放激素（LH-RH），并通过FAB质谱法进行分析。该方法提供了有关N端结构的直接信息。这些肽的N端焦谷氨酸在每个肽0.9 - 2.8 nmol的水平上被明确测定。消除了传统方法应用中伴随的几个复杂程序和争议。我们描述了FAB质谱法与焦谷氨酸氨肽酶消化相结合的程序在修饰氨基酸测定方面的优势。
