Chuknyiski P P, Alston K, Rifkind J M
Biochem Biophys Res Commun. 1985 Apr 30;128(2):721-7. doi: 10.1016/0006-291x(85)90106-8.
Temperature dependent absolute and difference spectra for deoxy and oxy human hemoglobin, alpha and beta subunits, NiHbA, carboxypeptidase A treated deoxy HbA and NiHbA have been investigated. It is shown for the first time that the alpha subunits are mainly responsible for the temperature dependent spectral changes in the absorption spectra of Hb in the range from 0 degrees C to 40 degrees C. It has also been found that in the R state the spectral alterations caused by temperature variation are about 85% of those found for the T state of Hb. The value of following the temperature dependence of the porphyrin bands of hemoproteins, as a sensitive probe for subtle changes in the region of the heme, is demonstrated.
已对脱氧和氧合人血红蛋白、α和β亚基、镍血红蛋白A、羧肽酶A处理的脱氧血红蛋白A和镍血红蛋白A的温度依赖性绝对光谱和差光谱进行了研究。首次表明，在0摄氏度至40摄氏度范围内，α亚基是血红蛋白吸收光谱中温度依赖性光谱变化的主要原因。还发现，在R状态下，温度变化引起的光谱改变约为血红蛋白T状态下光谱改变的85%。作为血红素区域细微变化的灵敏探针，追踪血蛋白卟啉带的温度依赖性的价值得到了证明。
