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Kil, Mee-Wha,Chang, Soo-Ik Korean Society for Biochemistry and Molecular Biol 1998 Journal of biochemistry and molecular biology Vol.31 No.3
Acetolactate synthase (ALS) is the first common enzyme in the biosynthesis of L-Ieucine, L-isoleucine, and L-valine. The sulfonylurea-resistant ALS gene from Nicotiana tabacum was cloned into the bacterial expression vector pGEX-2T. The resulting recombinant plasmid pGEX-ALS3 was used to transform Escherichia coli strain XL1-Blue, and the mutant tobacco ALS (mALS) was expressed in the bacteria as a protein fused with glutathione S-transferase (GST). The fusion product GST-mALS was purified in a single step on a glutathione-Sepharose column. ALS activities of 0.9-2.5 ${\mu}mol/min/mg$ protein were observed in the GST-mALS, and the Km values for pyruvate, FAD, and TPP were 10.8-24.1, $(1.9-8.9){\times}10^{-3}$, and 0.14-0.38 mM, respectively. The purified GST-mALS was resistant to both the sulfonylurea and the triazolopyrimidine herbicides, and lost its sensitivity to end products, L-valine and L-leucine. For comparision, the tobacco wild-type recombinant ALS fused with GST, GST-wALS, was also characterized with respect to its pyruvate and cofactor bindings. These results suggest that the purified mutant recombinant tobacco ALS was functionally active, that the mutations resulting in herbicide resistance has affected pyruvate and cofactor bindings," and that the two classes of herbicides interact at a common site on the plant ALS.
(Mee Wha Kil),(Soo Ik Chang) 생화학분자생물학회 1998 BMB Reports Vol.31 No.3
Acetolactate synthase (ALS) is the first common enzyme in the biosynthesis of L-leucine, L-isoleucine, and L-valine. The sulfonylurea-resistant ALS gene from Nicotiana tabacum was cloned into the bacterial expression vector pGEX-2T. The resulting recombinant plasmid pGEX-ALS3 was used to transform Escherichia coli strain XL1-Blue, and the mutant tobacco ALS (mALS) was expressed in the bacteria as a protein fused with glutathione S-transferase (GST). The fusion product GST-mALS was purified in a single step on a glutathione-Sepharose column. ALS activities of 0.9-2.5 μ㏖/min/㎎ protein were observed in the GST-mALS, and the K_m values for pyruvate, FAD, and TPP were 10.8-24.1, (1.9-8.9) × 10^(-3), and 0.14-0.38 mM, respectively. The purified GST-mALS was resistant to both the sulfonylurea and the triazolopyrimidine herbicides, and lost its sensitivity to end products, L-valine and L-leucine. For comparision, the tobacco wild-type recombinant ALS fused with GST, GST-wALS, was also characterized with respect to its pyruvate and cofactor bindings. These results suggest that the purified mutant recombinant tobacco ALS was functionally active, that the mutations resulting in herbicide resistance has affected pyruvate and cofactor bindings, and that the two classes of herbicides interact at a common site on the plant ALS.
정상과 갑상선 종양조직에서 사람 IGF-I 유전자의 발현
홍성화,김진우,고석환,최영길,김영설,김광원,양인명,우정택,김성운,김덕윤,장현하,박상미 대한내분비학회 1993 Endocrinology and metabolism Vol.8 No.4
Many of the growth-promoting properties of growth hormone (GH) are mediated by insulin-like growth factor-I (KGF-I), a highly conserved circulation 70-amino ackd peptide. Recent studies have shown that multiple mechanisms influence IGF-I gene expression, including trascription from two pormoters, alternative RNA splicing and variable polyadenylation. In thyroid tissue, thyroid stimulating hormone (TSH) and TGF-I are the most possible candidates for follicular cell proliferation and hypertrophy. Actually IGF-I had autocrine and paracrine effect for tissue growing. We prepared thyroid tumor tissue mRNAs using single step method for detecting IGF-I levels according to different tissue, I, e, thyroid adenoma or papillary thyroid carcinoma. We used Northern blot analysis for IGF-I mRNA and Rnase protection assay (RPA) for IGF-I transcription start sites. For Northern blot, we used whole human IGF-I cDNA as a DNA probe and for RPA, we used IGF-I exon 1 containing noncoding promoter 1 as a riboprobe. We got good RNA bands from Northern blot analysis around 1 kb(IGF-I A) and 7.5 kb(IGF-I B) region. To clarify the amount of both IGF-IA and IB mRNAs, we measured autoradinographied signal of IGF-a mRNA's bands using densitometer. In IGF-IA signals, there's no change among liver and thyroid tissues, but in case of IGF-IB mRNA bands, thd signal was markedly increased in thyroid carcinoma tissues than that of normal thyroid tissue (85% vs 14%). In the study of RPA, aoo thyroid tissues used the same transcription start sites as those of liver's. We concluded that that this different regulation of IGF-I mRNA was originated from tissue specificity. That meant some tissue specific transcription factors were related to tissue IGF-I -Sung Woon Kim, et al. : Human IGF-I Gene Expression in Normal and Thyroid Tumor Tissues- expression (J Kor Soc Endocrinol 8: 414~421, 1993).
Chang, Soo-Ik,Kil, Mee-Wha The Korea Science and Technology Center 1998 BMB Reports Vol.31 No.3
Acetolactate synthase (ALS) is the first common enzyme in the biosynthesis of L-leucine, L-isoleucine, and L-valine. The sulfonylurea-resistant ALS gene from Nicotiana tabacum was cloned into the bacterial expression vector pGEX-2T. The resulting recombinant plasmid pGEX-ALS3 was used to transform Escherichia coli strain XL 1-Blue, and the mutant tobacco ALS(mALS) was expressed in the bacteria as a protein fused with glutathione S-transferase (GST). The fusion product GST-mALS was purified ina single step on a glutathione-Sepharose column. ALS activities of 0.9-2.5 μmol/min/mg protein were observed in the GST-mALS, and the Km values for pyruvate, FAD, and TPP were 10.8-24.1, (1.9-8.9)×10-³, and 0.14-0/38 mM, respectively. The purified GST-mALS was resistant to both the sulfonylurea and the triazolopyrimidine herbicides, and lost its sensitivity to end products, L-valine and L-leucine. For comparision, the tobacco wild-type recombinant ALS fused with GST, GST-wALS, was also characterized with respect to its pyruvate and cofactor bindings. These results suggest that the purified mutant recombinant tobacco ALS was functionally active, that the mutations resulting in herbicide resistance has affected pyruvate and cofactor bindings, and that the two classes of herbicides interact at a common site on the plant ALS.
이숙영,이은화,이미정,채기준,최길영,강훈,Lee, Sook-Young,Lee, Eun-Wha,Lee, Mee-Jeong,Chae, Ki-Joon,Choi, Kil-Young,Kang, Hun 한국시뮬레이션학회 1997 한국시뮬레이션학회 논문지 Vol.6 No.2
MAC (media access control) bridge is used to interconnect separate LANs and to relay frames between the BLANs (bridged LANs). Bridge architecture consists of MAC entity, MAC relay entity and bridge protocol entity protocol entity and performs learning, filtering and forwarding functions using filtering database. In this paper, we simulate these functions of bridge and the STP (spanning tree protocol). The STP derives an active topology from an arbitrarily connected BLAN. Our simulation model assumes a BLAN consisted of three bridge forming a closed loop. In order to remove the loop, each bridge process exchanges configruation BPDU (bridge protocol data unit0 with other bridge processes connected to the bridge itself. To simulate the communication between bridges, we implement the IPC (inter-process communication) server using message queues. Our simulation results show that the assumed BLAN contains no closed loop and then there is no alternative route and no unnecessary traffic.
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.
Expression in Escherichia coli of a Putative Human Acetohydroxyacid Synthase
(Ronald G . Duggleby),(Apriliana E . R . Kartikasari),(Rebecca M . Wunsch),(Yu Ting Lee),(Mee Wha Kil),(Ju Young Shin),(Soo Ik Chang) 생화학분자생물학회 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 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.
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.