Kubal G, Mason A B, Sadler P J, Tucker A, Woodworth R C
Department of Chemistry, Birkbeck College, University of London, U.K.
Biochem J. 1992 Aug 1;285 ( Pt 3)(Pt 3):711-4. doi: 10.1042/bj2850711.
We have studied the binding of Al3+ to human serum apotransferrin (80 kDa) and recombinant N-lobe human apotransferrin (40 kDa) in 0.1 M-sodium bicarbonate solution at a pH meter reading in 2H2O (pH*) of 8.8 using 1H n.m.r. spectroscopy. The results show that for the intact protein, preferential binding of Al3+ to the N-lobe occurs. Molecular modelling combined with an analysis of ring-current-induced shifts suggest that n.m.r. spectroscopy can be used to probe hinge bending processes which accompany metal uptake in solution.
我们使用核磁共振光谱法，在pH*为8.8的重水（2H2O）中，于0.1M碳酸氢钠溶液中研究了Al3+与人类血清脱铁转铁蛋白（80 kDa）以及重组N-叶人类脱铁转铁蛋白（40 kDa）的结合情况。结果表明，对于完整的蛋白质，Al3+优先与N-叶结合。分子建模结合对环电流诱导位移的分析表明，核磁共振光谱可用于探测溶液中金属摄取过程中伴随的铰链弯曲过程。
