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현제 우리나라 HMG-COA reductase 관련 논문중 가장 정확하며 가장 최근의 자료이며 SCI에 등제된 논문이며 가장 쉽게 이해하실수 있을것입니다.목차
IntroductionⅡ. Materials and Methods
1. Medicinal plants, strain and chemicals
2. Buffer solution and media
3. Extraction of medicinal plants
4. Assay of HMG-CoA reductase inhibitory activity
1) Preparation and purification of Syrian
hamster HMG-CoA reductase
2) Assay of HMG-CoA reductse inhibitory
activity
5. Purification and characterization of HMG-
CoA reductase inhibitor
1) Thin layer chromatography and silica gel
column chromatography
2) High performance liquid chromatography
① Reverse phase HPLC
② Preparative HPLC
③ Analytical HPLC1212
3) LC/Mass spectrometry
4) 1H, 13C-NMR spectrometry
5) Fourier Transform-Infrdred(FT-IR) spectro-
metry
Ⅲ. Results and Discussion
1. Solid yield of various extracts
2. HMG-CoA reductase inhibitory activity of
various extracts
3. Optimal condition for extraction of the HMG
-CoA reductase inhibitor
4. Purification of the HMG-CoA reductase
inhibitor
1) Systematic solvent extraction and silica gel
column chromatography
2) High performance liquid chromatography33
5. Characteristics of the purified HMG-CoA
reductase inhibitor
1) M.W and structure
2) Physico-chemical properties
3) Inhibition kinetics of the purified HMG-CoA
reductase inhibitor
6. Antihyperlipemia action in Vero cells
Ⅳ. Conclusion
Ⅴ. References
ABSTRACT IN KOREAN
본문내용
Ⅰ. IntroductionExtensive epidemiological studies performed in many countries have shown increased blood cholesterol levels, or more specifically, increased coronary heart disease. There is also substantial evidence that lowering total cholesterol and low density lipoprotein (LDL) cholesterol levels will reduce the incidence of coronary heart disease.(Bichhoff et al. 1992, 1996)
HMG-CoA reductase (E.C 1.1.1.34), the rate-limiting enzyme in endogenous cholesterol synthesis is 97KDa glycoprotein and catalyses the reductive deacylation of HMG-CoA to mevalonate in a two-step reaction.(Daniel et al. 1999, Frimpong et al. 1993, 1994) The stereospecificity of HMG-CoA reductase was illustrated in Fig. 1. A finely tuned mechanism modulates the biosynthesis of mevalonate, the precursor of isoprenoid group that are incorporated into more than a dozen classes of end-products(Fig. 2). These include sterols, especially cholesterol, involved in membrane structure; heam A an ubiquinone, which partake in electron tansport ; dolichol required for glycoprotein synthesis ; isopentyladeine, present in some transfer RNAs; and intercellular messengers, such as cytokines in plants, farneylated mating factors in
참고 자료
Ⅴ. ReferencesAOAC. Offical Methods of Analysis, 15th edition, Asso-
ciation of Offical Analytical Chemists, Inc. Washington, DC, USA(1990)
Bischoff, K. M., and V. W. Rodwell. 3-Hydroxy-3-met
hylglutaryl-CoA reductase from Haloferax volcanii. Role of histidine 398 and attenuation of activity by introduction of negative charge at position 404. Protein Science, 6, 156-161(1997)
Bischoff, K. M., and V. W. Rodwell. Biosynthesis and
isolation of (S)- and (R)-3-hydroxy-3-methylglutaryl coenzyme A. Biochem. Med. Metab. Biol. 48, 149-158 (1992)
Bischoff, K. M., and V. W. Rodwell. 3-Hydroxy-3-me
thylglutaryl-CoA reductase from Haloferax volcanii.
Purification, characterization, and expression in Escherichia coli. J. Bacteriol. 178, 19-23(1996)
Darnay, B. G., and V. W. Rodwell. His865 is the catalytically important histidyl residue of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Biol. Chem. 268, 8429-8435 (1993)
Darnay, B. G., Y. Wang, and V. W. Rodwell. Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Biol. Chem. 267, 15064-15070 (1992)
Daniel A. Bochar, Cynthia V. Stauffacher, and Victor
W. Rodwell. Investigation of the conserved lysines of Syrian hamster 3-hydroxy-3-methylglutaryl coenzme A reductase. Biochemistry 38, 15848-15852 (1999)
Daniel A. Bochar, Lydia Tabernero, Cynthia V. Stauffacher, and Victor W. Rodwell. Aminoethylcyste-
ine can replace the active site lysine of Pseudomonas
mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase. Biochemistry 38, 8879-8883(1999)
Daniel A. Bochar, James R. Brown, W. Ford Doolittle, Hans-Peter Klenk, Wan Lam, Maragret E. Schenk, Cynthia V. Stauffacher, and Victor W. Rodwell. 3-Hydroxy-3-methylglutaryl coenzyme A reductase of Sulfolobus solfataricus: DNA sequence, phylogeny, expression in Escherichia coli of the hmgA gene, and purification and kinetic characterization of the gene product. J. Bacteriol. 179, 3632-3638 (1997).
Endo, A., HMG-CoA reductase inhibitors., Natural Products Reports , 10. 541-550
Frimpong, K., and V. W. Rodwell. Catalysis by Syrian hamster 3-hydroxy-3-methylglutaryl-CoA reductase. Proposed roles of histidine 865, glutamate 558, and aspartate 766. J. Biol. Chem. 269, 11478-
11483(1994)
Frimpong, K., B. G<font color=aaaaff>..</font>
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