Takao T, Yoshino K, Suzuki N, Shimonishi Y
Institute for Protein Research, Osaka University, Japan.
Biomed Environ Mass Spectrom. 1990 Nov;19(11):705-12. doi: 10.1002/bms.1200191109.
A rotatable dual-target probe was used for accurate mass measurement in fast atom bombardment mass spectrometry to determine the structures of unknown amino acid residues or post-translationally modified structures in peptides or proteins. The results obtained in measurement of tryptic peptides (with molecular weights of up to 2000) of the A-subunit of vero-toxin I indicated that the mass values obtained are sufficiently accurate and reproducible to allow the generation of the possible elemental compositions for modifications in peptides. By this method, the structural modifications of the N-terminal of a recombinant human leukocyte interferon A and novel halogenated amino acids in sperm-activating peptides from the egg-jelly of sea urchins were determined.
一种可旋转的双靶点探针用于快速原子轰击质谱中的精确质量测量，以确定肽或蛋白质中未知氨基酸残基或翻译后修饰结构的结构。在对 vero-毒素 I 的 A 亚基的胰蛋白酶肽（分子量高达 2000）进行测量时获得的结果表明，所获得的质量值足够准确且可重复，从而能够生成肽中修饰的可能元素组成。通过这种方法，确定了重组人白细胞干扰素 A 的 N 端的结构修饰以及海胆卵胶中精子激活肽中的新型卤代氨基酸。
