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Effects of Different Valences of Cerium Ion on Conformation of Horseradish Peroxidase
Author: XiangLi
Tutor: GeZhiQiang
School: Tianjin University
Course: Biochemical Engineering
Keywords: Cerium ions Conformation Horseradish peroxidase Heme
CLC: Q943.1
Type: Master's thesis
Year: 2007
Downloads: 51
Quote: 0
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Abstract
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In suspension cultures of Taxus cuspidata cells, Ce 4 sup> as elicitors promote signaling molecules thereby increasing the oxidative burst activity of taxol production. In order to investigate the Ce 4 sup> as elicitors affect cell oxidoreductases structure and function and may regulate the mechanism of oxidative burst activity, this paper Ce 4 sup> and Ce 3 < / sup> under the action of horseradish peroxidase conformational change as the starting point, the integrated use of a variety of detection methods at the molecular level for a more comprehensive study, achieved the following results: (1) Ce 4 sup> than Ce 3 sup> more effectively change the horseradish peroxidase enzymatic reaction kinetics, enzyme activity, the maximum reaction rate and the affinity of the enzyme and substrate are as Ce < sup> 4 sup> and Ce 3 sup> concentration increases gradually reduced. (2) Application of UV spectrophotometer, fluorescence spectrophotometer, and electronic paramagnetic resonance for Ce 4 sup> and Ce 3 sup> Induced three horseradish peroxidase level study the structure, the Ce 4 sup> and Ce 3 sup> horseradish peroxidase after natural state with different spectral characteristics, and this change with Ce < sup> 4 sup> and Ce 3 sup> concentration increased more apparent. Although Ce 4 sup> and Ce 3 sup> horseradish peroxidase caused by UV absorption peaks same trend, but Ce 4 sup> caused characteristic peak shift and intensity changes are stronger than Ce 3 sup>; and Ce 4 sup> and Ce 3 sup> tryptophan fluorescence emission peaks caused by the trend Conversely, g factor values ??are also significant differences. (3) by means of circular dichroism and Fourier transform infrared spectroscopy and data to be found, Ce 4 sup> and Ce 3 sup> makes horseradish peroxidase relative percentage of the secondary structure content changes, the balance from the α helix angle β and β folding movement. The transformation between two structures for Ce 4 sup> and Ce 3 sup> with a concentration-dependent manner; and under the same conditions Ce 4 sup> caused by the degree of conversion much larger than Ce 3 sup>. Ce 4 sup> and Ce 3 sup> for horseradish peroxidase secondary and tertiary structures of different possible impact to their ionic radii, pros and cons of electronic capabilities, charges related to the different arrangement. Ce 4 sup> as elicitors promote ROS burst may be related peroxidase secondary and tertiary structure of affect.
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