摘要
重组人源性抗HBsAg Fab抗体具有较好的特异性和抗原结合活性,为了更好的阐明毕赤 酵母表达的重组人源性抗HBsAg Fab抗体的性质,用基质辅助激光解析飞行时间质谱(MALDI- TOF-MS)对重组Fab抗体的分子质量和肽质量图谱进行了分析。结果显示,毕赤酵母表达的重组 人源性抗HBsAg Fab抗体的分子质量为50678．49Da,与根据其一级结构计算的理论分子质量相 比多2763．84 Da,显示酵母表达的重组Fab抗体为糖蛋白。用胰蛋白酶酶解重组Fab抗体后进行 MALDI-TOF-MS分析显示,大部分的酶解肽段均能检测出来。结果表明毕赤酵母表达的重组Fab 抗体与预期的结构一致。
The recombinant humanized anti-HBsAg Fab secreted from yeast cells has high antigen specificity and affinity activity, which could sufficiently neutralize the HBsAg. In order to clarify the character of the recombinant Fab, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry （MALDI-TOF-MS） was used to analyze the molecular mass and peptide mass spectrum. The results showed that the molecular mass of recombinant Fab was 50678.49 Da, which is 2763.84 Da higher than the calculated value. The recombinant Fab was treated by trypsin and analyzed by MALDI-TOF-MS. The most peptides could be found. The results indicated that the recombinant humanized anti-HBsAg Fab was constructed correctly.
出处
《中国生物工程杂志》
CAS
CSCD
北大核心
2005年第B04期224-227,共4页
China Biotechnology
基金
国家自然科学基金资助项目(30471607)广州市科技局重点资助项目(2003J1-CO171)
