通过基质辅助激光解吸电离飞行时间质谱法分析汽巴克隆蓝F3G-A与治疗性蛋白质的相互作用。
Analysis of Cibacron blue F3G-A interaction with therapeutic proteins by MALDI-TOF mass spectrometry.
作者信息
Sutkeviciute Ieva, Sereikaite Jolanta, Bumelis Vladas-Algirdas
机构信息
Department of Chemistry and Bioengineering, Vilnius Gediminas Technical University, Vilnius, Lithuania.
出版信息
Biomed Chromatogr. 2008 Sep;22(9):1001-7. doi: 10.1002/bmc.1019.
The formation of the complexes between Cibacron blue F3G-A and two therapeutic proteins, recombinant human interferon-alpha2b and recombinant human growth hormone, was investigated. The method of time-resolved limited proteolysis coupled with MALDI-TOF mass spectrometry was used. The analysis of peptide maps revealed that A(17)HR(19) and L(20)HQLAFDTYQEFEEAYIPK(38) of hGH, and R(14)TLMLLAQMR(23) and D(33)RHDFGFPQEEFGNQFQK(50) of hIFN-alpha2b, exhibit affinity to Cibacron blue F3G-A.
研究了汽巴克隆蓝F3G-A与两种治疗性蛋白质，即重组人干扰素α2b和重组人生长激素之间复合物的形成。采用了时间分辨有限蛋白酶解结合基质辅助激光解吸电离飞行时间质谱法。肽图分析表明，人生长激素的A(17)HR(19)和L(20)HQLAFDTYQEFEEAYIPK(38)，以及人干扰素α2b的R(14)TLMLLAQMR(23)和D(33)RHDFGFPQEEFGNQFQK(50)对汽巴克隆蓝F3G-A具有亲和力。
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