Kostiainen R, Lasonder E, Bloemhoff W, van Veelen P A, Welling G W, Bruins A P
University Centre for Pharmacy, Groningen, The Netherlands.
Biol Mass Spectrom. 1994 Jun;23(6):346-52. doi: 10.1002/bms.1200230608.
A peptide comprising 37 amino acids of the antigen binding site of a monoclonal antibody directed against glycoprotein D of herpes simplex virus was synthesized. The synthetic peptide and the impurities formed in the synthesis were characterized by capillary electrophoresis/ionspray mass spectrometry and by 252Cf plasma desorption-time of flight mass spectrometry. The measured average molecular mass of the synthetic peptide was 4627.16 Da, which was only 0.08 Da higher than the calculated value (4627.08 Da). The plasma desorption mass spectrum of the synthetic peptide showed a protonated molecule at m/z 4624.1, which was 4 Da lower than the calculated one (4628.09 Da). The amino acid sequence of the peptide was confirmed in part by electrospray (ionspray) mass spectrometry using a high nozzle skimmer voltage difference. Five impurities were separated and identified by capillary electrophoresis/mass spectrometry and two of them also appeared in the plasma desorption mass spectrum.
合成了一种包含针对单纯疱疹病毒糖蛋白D的单克隆抗体抗原结合位点37个氨基酸的肽。通过毛细管电泳/离子喷雾质谱法和252Cf等离子体解吸飞行时间质谱法对合成肽及其合成过程中形成的杂质进行了表征。合成肽的实测平均分子量为4627.16 Da，仅比计算值（4627.08 Da）高0.08 Da。合成肽的等离子体解吸质谱显示，在m/z 4624.1处有一个质子化分子，比计算值（4628.09 Da）低4 Da。使用高喷嘴分离器电压差通过电喷雾（离子喷雾）质谱法部分确认了该肽的氨基酸序列。通过毛细管电泳/质谱法分离并鉴定了五种杂质，其中两种也出现在等离子体解吸质谱中。
