Fenselau C, Heller D N, Miller M S, White H B
Anal Biochem. 1985 Nov 1;150(2):309-14. doi: 10.1016/0003-2697(85)90515-9.
The capability of fast atom bombardment mass spectrometry for characterization of phosphorylation sites in a tryptic peptide from chicken egg yolk riboflavin-binding protein has been evaluated. The quality of information about molecular weight, amino acid sequence, phosphorylation sites, and microheterogeneity is evaluated as a function of the sign of the ions analyzed, the nature of the counter ions associated with the phosphate substituents, sample matrix, and various instrumental parameters. The intact octaphosphorylated 23-residue peptide was found to be susceptible to mass spectral analysis. Information from the negative ion spectrum was used in conjunction with complete sequence information and experiments which showed that all phosphates were attached to serine residues. Phosphorylated and unphosphorylated serine residues were identified and the sample was shown to be homogeneously octaphosphorylated.
已评估了快原子轰击质谱法对鸡卵黄核黄素结合蛋白胰蛋白酶解肽中磷酸化位点进行表征的能力。作为所分析离子的符号、与磷酸取代基相关的抗衡离子的性质、样品基质以及各种仪器参数的函数，对有关分子量、氨基酸序列、磷酸化位点和微不均一性的信息质量进行了评估。发现完整的八磷酸化23个残基的肽易于进行质谱分析。负离子谱的信息与完整的序列信息以及实验相结合使用，实验表明所有磷酸盐均连接到丝氨酸残基上。鉴定出了磷酸化和未磷酸化的丝氨酸残基，并且样品显示为均一的八磷酸化。
