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Inverstigation of Sulfhydryl Oxidases and Their Probes

Author: HuZuo
Tutor: YangZuo
School: East China University of Science and Technology
Course: Biochemistry and Molecular Biology
Keywords: HQSOX protein Copepod luciferase BRET FRET
CLC: Q55
Type: Master's thesis
Year: 2011
Downloads: 52
Quote: 0
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Abstract


Resting sulfhydryl oxidase QSOX family belongs to a class FAD binding thiol oxidase, which as a disulfide bond -forming enzyme protein intracellular oxidative folding a lot of play a crucial role . This QSOX of human recombinant protein (HsQSOX protein) of the structure and function of a series of studies . In the full-length protein HQSOX (30-604) on the basis of studies reported in the literature HsQSOX by referring to the secondary structure of proteins , amino acid sequence and structure of the domain information, the use of molecular biology methods for the series truncated plasmids , carried out in E. coli expression and purification of these truncated proteins and TCEP, DTT and rRNase three kinds of substrate oxidation reduction activity detection , the final confirmation of the oxidation activity for TCEP has the smallest domain protein is HQSOX (295 - 536 ) , and argues HsQSOX various domains of the protein missing the oxidation activity. HsQSOX under in vivo conditions in order to detect the catalytic function can copepod luciferase (gaussia luciferase) Gluc thiol oxidation as a probe . Gluc protein contains nine cysteines , in the case of completely oxidized to form a four disulfide bonds , but only Gluc protein disulfide bonds are oxidized only in the activity , so it is a good functioning of the activity bad direct proof HsQSOX oxidation Gluc protein thiol degree, but in vivo gaussia luciferase protein to the substrate under the action of the emitted blue light easily through the cell membrane and therefore require the use of BRET and in FRET their emitted light into ETAN membrane red cells indirectly reflect the light, and thus reflect the catalytic function HsQSOX protein . In this paper, Gluc, mKO2, mCherry nature and function of the three proteins , light emission is obtained by mutation of prolonged Gluc mutant protein and a series of different lengths by constructing a fusion protein linker tablets, to be transformed into E. coli in the small expression in the cell supernatant after crushing for BRET and FRET phenomena , eventually won the FRET phenomenon obviously a fusion protein in vivo detection HsQSOX and Gluc protein function basis.

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CLC: > Biological Sciences > Biochemistry > Enzymes
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