Savicki J P, Lang G, Ikeda-Saito M
Proc Natl Acad Sci U S A. 1984 Sep;81(17):5417-9. doi: 10.1073/pnas.81.17.5417.
The room temperature magnetic susceptibilities of human and carp oxy- and carbonmonoxyhemoglobin solutions were measured in a 30-gauss (1 G = 10(-4) T) field with a superconducting magnetometer. To within experimental uncertainty, the susceptibility was the same for both the oxy and carbonmonoxy forms, and salt concentration did not effect it. A variety of sample preparations were used; the iron chemical state was verified by Mössbauer spectroscopy. A value of -0.580 +/- 0.010 X 10(-6) centimeter-gram-second (cgs) system was obtained for the mass susceptibility of the protein. We attribute the paramagnetism sometimes observed in oxyhemoglobin solutions to the presence of a small amount of the deoxy form.
使用超导磁力计在30高斯(1 G = 10⁻⁴ T)的磁场中测量了人和鲤鱼的氧合血红蛋白及碳氧血红蛋白溶液在室温下的磁化率。在实验误差范围内,氧合形式和碳氧形式的磁化率相同,盐浓度对其没有影响。使用了多种样品制备方法;通过穆斯堡尔光谱法验证了铁的化学状态。蛋白质的质量磁化率值为-0.580±0.010×10⁻⁶厘米 - 克 - 秒(cgs)制。我们将有时在氧合血红蛋白溶液中观察到的顺磁性归因于少量脱氧形式的存在。