Vermeer A W, Norde W, van Amerongen A
Laboratory for Physical Chemistry and Colloid Science, Wageningen University, 6703 HB Wageningen, The Netherlands.
Biophys J. 2000 Oct;79(4):2150-4. doi: 10.1016/S0006-3495(00)76462-9.
The unfolding and further denaturation of IgG and its F(ab) and F(c) fragments were studied both on a macroscopic and molecular level, using differential scanning calorimetry and circular dichroism spectroscopy, respectively. It was shown that the structural integrity of the F(ab) and F(c) units was retained after fragmentation of the IgG. The F(ab) fragment denatured at approximately 61 degrees C and the F(c) fragment at 71 degrees C. The structural transitions observed in the whole IgG is the sum effect of those determined for the isolated F(ab) and F(c) fragments.
分别使用差示扫描量热法和圆二色光谱法，在宏观和分子水平上研究了IgG及其F(ab)和F(c)片段的展开和进一步变性。结果表明，IgG片段化后，F(ab)和F(c)单元的结构完整性得以保留。F(ab)片段在约61℃变性，F(c)片段在71℃变性。在整个IgG中观察到的结构转变是分离的F(ab)和F(c)片段所确定的结构转变的总和效应。
