Toselli M, Battistel E, Manca F, Rialdi G
Biochim Biophys Acta. 1981 Jan 30;667(1):99-107. doi: 10.1016/0005-2795(81)90070-2.
The reaction of concanavalin A with Mn2+ has been studied calorimetrically. The binding enthalpy was measured at two different temperatures, 25 and 30 degrees C, in 10(-3) M acetate buffer; it was found to be constant between pH 4.0 and 5.0, delta H250 = 95 kJ/mol and delta H300 = 65 kJ/mol, respectively. The two S1 binding sites are identical and independent. Experiments at pH 5.6 are distorted by the heat of aggregation, which is several times higher than the heat of binding. Aggregation was demonstrated by spectrophotometric experiments and by light scattering. The presence of Mn2+ increases the stability of the protein molecule.
已用量热法研究了伴刀豆球蛋白A与Mn2+的反应。在10^(-3) M醋酸盐缓冲液中，于25和30摄氏度这两个不同温度下测量了结合焓；发现在pH 4.0至5.0之间其保持恒定，δH250 = 95 kJ/mol，δH300 = 65 kJ/mol。两个S1结合位点相同且相互独立。在pH 5.6下进行的实验因聚集热而受到干扰，聚集热比结合热高几倍。通过分光光度实验和光散射证明了聚集现象。Mn2+的存在增加了蛋白质分子的稳定性。
