Department of Physics, Annamalai University, Annamalai Nagar 608002, Tamil Nadu, India.
Environ Toxicol. 2010 Feb;25(1):61-7. doi: 10.1002/tox.20475.
In the present study, an attempt has been made to analyze the changes in the biochemical and mineral contents of lead-intoxicated bones of Catla catla at subchronic (15.5 ppm) exposure, and also to determine whether the effects of Pb intoxication can be reversed with the chelating agent meso 2, 3-dimercaptosuccinic acid (DMSA) on the bones of freshwater fingerlings Catla catla by using Fourier transform infrared (FT-IR) spectroscopy, X-ray diffraction (XRD), and atomic absorption spectrophotometer techniques. The FT-IR spectra of the lead-exposed bones show significant alteration in the biochemical constituents. The XRD analysis showed a decrease in crystallinity due to lead exposure. Further, the Ca, Mg, and P contents of the lead-exposed bones were less than those of the control group, and there was an increase in the mineral contents of the bones after DMSA treatment. In conclusion, the present study suggests that the subchronic lead exposure results in severe loss of bone minerals. The overall decrease in the FT-IR band intensity of Pb-exposed bones relative to the control indicates a decrease in the biochemical constituents like proteins and lipids. The increase in the band intensity after treatment with chelating agent DMSA indicates increased biochemical constituents, showing that the subchronic effects of lead can be reversed by DMSA. The amide I bands observed at 1654 cm(-1) in the present study suggest that the protein is dominated by alpha-helical structure.
在本研究中,尝试分析了 Catla catla 骨骼在亚慢性(15.5ppm)铅暴露下的生化和矿物质含量的变化,并确定螯合剂 meso 2,3-二巯基丁二酸(DMSA)是否可以逆转 Pb 中毒对淡水鱼苗 Catla catla 骨骼的影响,方法是使用傅里叶变换红外(FT-IR)光谱、X 射线衍射(XRD)和原子吸收分光光度法技术。铅暴露骨骼的 FT-IR 光谱显示生化成分发生了显著变化。XRD 分析表明,由于铅暴露,结晶度降低。此外,铅暴露骨骼的 Ca、Mg 和 P 含量低于对照组,而 DMSA 处理后骨骼的矿物质含量增加。总之,本研究表明,亚慢性铅暴露会导致严重的骨质矿物质流失。与对照组相比,Pb 暴露骨骼的 FT-IR 带强度整体降低表明生化成分(如蛋白质和脂质)减少。螯合剂 DMSA 处理后带强度增加表明生化成分增加,表明 DMSA 可以逆转铅的亚慢性影响。本研究中观察到的 1654cm(-1)处的酰胺 I 带表明蛋白质主要由α-螺旋结构组成。