Kakar S, Bettelheim F A
Chemistry Department, Adelphi University, Garden City, NY 11530.
Invest Ophthalmol Vis Sci. 1991 Mar;32(3):562-6.
The hydration of actin was studied by differential scanning calorimetry between -30 degrees C and 30 degrees C and by thermogravimetric analysis. The differential scanning calorimetry provided the freezable water content of G- and F-actin as a function of concentration, and the thermogravimetric analysis measured the total water content. The difference between the two yielded the nonfreezable water content (bound water) as a function of concentration. The nonfreezable water content of G-actin was higher than the F-actin over the whole concentration range from 1-40% actin.
通过差示扫描量热法在-30℃至30℃之间以及热重分析法研究了肌动蛋白的水合作用。差示扫描量热法给出了G-肌动蛋白和F-肌动蛋白的可冷冻水含量随浓度的变化情况，热重分析法测量了总含水量。两者的差值得出了不可冷冻水含量（结合水）随浓度的变化情况。在肌动蛋白浓度为1%-40%的整个范围内，G-肌动蛋白的不可冷冻水含量高于F-肌动蛋白。
