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Expression in Escherichia coli of a Putative Human Acetohydroxyacid Synthase
Chang,Soo-Ik,Kartikasari,Apriliana E.R.,Wunsch,Rebecca M.,Lee,Yu-Ting,Kil,Mee-Wha,Shin,Ju-Young,Duggleby,Ronald G. The Korea Science and Technology Center 2000 BMB Reports Vol.33 No.3
A human gene has been reported that may encode the enzyme acetohydroxyacid synthase. Previously this enzyme was thought to be absent from animals although it is present in plants and many microorganisms. In plants, this enzyme is the target of a number of commercial herbicides and the use of these compounds may need to be reassessed if the human enzyme exists and proves to be susceptible to inhibition. Here we report the construction of several plasmid vectors containing the cDNA sequence for this protein, and their expression in Escherichia coli. High levels of expression were observed, but most of the protein proved to be insoluble. The small amounts of soluble protein contained little or no acetohydroxyacid synthase activity. Attempt to refold the insoluble protein were successful insofar as the protein became soluble. However, the refolded protein did not gain any acetohydroxyacid synthase activity. In vivo complementation tests of an E. coli mutant produced no evidence that the protein is active. Incorrect folding, or the lack of another subunit, may explain the data but we favor the interpretation that this gene does not encode an acetohydroxyacid synthase.
Expression in Escherichia coli of a Putative Human Acetohydroxyacid Synthase
Duggleby, Ronald G.,Kartikasari, Apriliana E.R.,Wunsch, Rebecca M.,Lee, Yu-Ting,Kil, Mee-Wha,Shin, Ju-Young,Chang, Soo-Ik Korean Society for Biochemistry and Molecular Biol 2000 Journal of biochemistry and molecular biology Vol.33 No.3
A human gene has been reported that may encode the enzyme acetohydroxyacid synthase. Previously this enzyme was thought to be absent from animals although it is present in plants and many microorganisms. In plants, this enzyme is the target of a number of commercial herbicides and the use of these compounds may need to be reassessed if the human enzyme exists and proves to be susceptible to inhibition. Here we report the construction of several plasmid vectors containing the cDNA sequence for this protein, and their expression in Escherichia coli. High levels of expression were observed, but most of the protein proved to be insoluble. The small amounts of soluble protein contained little or no acetohydroxyacid synthase activity. Attempts to refold the insoluble protein were successful insofar as the protein became soluble. However, the refolded protein did not gain any acetohydroxyacid synthase activity. In vivo complementation tests of an E. coli mutant produced no evidence that the protein is active. Incorrect folding, or the lack of another subunit, may explain the data but we favor the interpretation that this gene does not encode an acetohydroxyacid synthase.
( Fauzi Febrianto ),( Dini Lestari ),( Adesna Fatrawana ),( Sena Maulana ),( Rita Kartikasari ),( I Nyoman Jaya Wistara ),( Deded Sarip Nawawi ),( Nam Hun Kim ) 韓國木材工學會 2017 한국목재공학회 학술발표논문집 Vol.2017 No.1
Dimensional stability and strength of bamboo oriented strand board (BOSB) were much improved when bamboo strands were steamed pre-treated prior to be mixed with adhesive. However, the treatment is still needs to be improved due to some extractives were still accumulated on the surfaces of strands. The objectives of this research were to evaluate physical, mechanical and durability properties of BOSB prepared from modified steam treatment of betung bamboo strand (Dendrocalamus asper) and chemical composition change during the treatment. Three layers of BOSB were prepared and the ratio of surface, core and back layer was set 1:1:1. The strands were steamed at closed tank at certain condition. Some strands were washed with distilled and NaOH 1% solution. Paraffin in amount of 1 % was added. A rotary drum blender was used for mixing the strands and 8% PF adhesive. The mat-form was hot-pressed at 135 ℃ for 10 min at a pressure of 2.5 MPa to fabricate BOSBs. The board was then conditioned for two weeks in a room condition. For comparison, BOSB prepared from strands preserved with 3% borax preservative was also developed. Steam treatment greatly improved dimensional stabilization i.e. water absorption (WA) and thickness swelling (TS) and mechanical properties i.e. MOE, MOR and internal bond (IB) of BOSB. Washing strands with NaOH 1% solution after steamed treatment resulted in better improvement of those parameters than washing with distilled water. BOSB resulted from the above modified steam processes also improved its durability against termite attacked. Extractives, holocellulose and lignin of bamboo reduced and pH value and alpha cellulose increased after applying steam. Durability class of BOSB obtained in this experiment was equal with using 3% borax preservative.
Expression in Escherichia coli of a Putative Human Acetohydroxyacid Synthase
Chang, Soo Ik,Duggleby, Ronald G .,Kil, Mee Wha,Kartikasari, Apriliana E . R .,Wunsch, Rebecca M .,Lee, Yu Ting,Shin, Ju Young 생화학분자생물학회 2001 BMB Reports Vol.33 No.3
A human gene has been reported that may encode the enzyme acetohydroxyacid synthase. Previously this enzyme was thought to be absent from animals although it is present in plants and many microorganisms. In plants, this enzyme is the target of a number of commercial herbicides and the use of these compounds may need to be reassessed if the human enzyme exists and proves to be susceptible to inhibition. Here we report the construction of several plasmid vectors containing the cDNA sequence for this protein, and their expression in Escherichia coli. High levels of expression were observed, but most of the protein proved to be insoluble. The small amounts of soluble protein contained tittle or no acetohydroxyacid synthase activity. Attempts to refold the insoluble protein were successful insofar as the protein became soluble. However, the refolded protein did not gain any acetohydroxyacid synthase activity. In vivo complementation tests of an E. coli mutant produced no evidence that the protein is active. Incorrect folding, or the lack of another subunit, may explain the data but we favor the interpretation that this gene does not encode an acetohydroxyacid synthase.