Maiti M, Kono M, Chakrabarti B
Eye Research Institute, Boston, MA 02114.
FEBS Lett. 1988 Aug 15;236(1):109-14. doi: 10.1016/0014-5793(88)80295-3.
Of the crystallin proteins of the lens, the principal subunit of the beta-crystallin, beta B2 (beta Bp), has been considered to be the only heat-stable protein because it does not precipitate upon heating. In our recent investigations, however, we have found that the alpha-crystallin from bovine lenses is not only heat stable but also does not denature at temperatures up to 100 degrees C. Using circular dichroism and fluorescence to monitor the conformational changes of alpha- and beta B2-crystallins upon heating, we found that alpha-crystallin maintains a high degree of structure, whereas the beta B2-crystallin shows a reversible sigmoidal order-disorder transition at about 58 degrees C.
在晶状体的晶状体蛋白中，β-晶状体蛋白的主要亚基βB2（βBp）被认为是唯一的热稳定蛋白，因为它在加热时不会沉淀。然而，在我们最近的研究中，我们发现牛晶状体中的α-晶状体蛋白不仅热稳定，而且在高达100摄氏度的温度下也不会变性。利用圆二色性和荧光来监测加热时α-和βB2-晶状体蛋白的构象变化，我们发现α-晶状体蛋白保持高度的结构，而βB2-晶状体蛋白在约58摄氏度时显示出可逆的S形有序-无序转变。
