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首页> 外文期刊>Luminescence: The journal of biological and chemical luminescence >Studies on the interaction of palmatine hydrochloride with bovine hemoglobin
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Studies on the interaction of palmatine hydrochloride with bovine hemoglobin

机译：盐酸巴马汀与牛血红蛋白相互作用的研究

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The interaction between bovine hemoglobin (BHb) and palmatine hydrochloride (PMT) was investigated at different temperatures using multispectroscopy, as well as the effect of common metal ions (Ca~(2+), Mg~(2+), Zn~(2+), Cu~(2+), Fe~(2+), Fe~(3+), Co~(2+), Ni~(2+)) on the BHb-PMT system. Results showed that the quenching mechanism of PMT on BHb was a static process. The electrostatic force played an important role in the conjugation reaction between BHb and PMT. The order of magnitude of the binding constants (K_a) was 10~4, and the number of binding sites (n) in the binary system was ~ 1. The binding distance (r) was ~ 2.44nm and the primary binding for PMT was located at β-37 tryptophan in the hydrophobic cavity of BHb. In addition, the Hill's coefficients were ~ 1. Synchronous and circular dichroism spectra revealed that the microenvironment and the conformation of BHb were changed during the binding reaction.
机译：使用多光谱技术研究了牛血红蛋白（BHb）与盐酸帕马汀（PMT）之间的相互作用以及常见金属离子（Ca〜（2 +），Mg〜（2 +），Zn〜（2 +），Cu〜（2 +），Fe〜（2 +），Fe〜（3 +），Co〜（2 +），Ni〜（2+））在BHb-PMT系统上。结果表明，PMT对BHb的淬灭机理是一个静态过程。静电力在BHb与PMT之间的共轭反应中起重要作用。结合常数（K_a）的数量级为10〜4，二元体系中的结合位点数（n）为〜1。结合距离（r）为〜2.44nm，对PMT的初次结合为位于BHb的疏水腔中的β-37色氨酸。此外，希尔的系数约为1。同步和圆二色性光谱表明，结合反应过程中BHb的微环境和构象发生了变化。

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