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Vengatesh Narmatha Bai,Rajendran Ananthan,Muniappan Latha,Leelavinothan Pari,Kunga Mohan Ramkumar,Chokkanna Gounder Baskar 한국식품영양과학회 2003 Journal of medicinal food Vol.6 No.1
The effects of Gymnema montanum , an endangered plant used in the ancient period of India,on blood glucose, plasma insulin, and carbohydrate metabolic enzymes were studied in al-loxan diabetic rats. Administration of alcoholic extract of G. montanum leaves (50, 10, 20mg/kg body weight) to alloxan diabetic rats for 3 weks reduced the blood glucose level. Ad-ministration of G. montanum leaf extract (GLEt) at 200 mg/kg body weight significantly de-creased the blood glucose levels and significantly increased the plasma insulin levels. Thisclearly shows the antidiabetic efficacy of GLEt, which was better than that of glibenclamide.43
Purification and Characterization of a Novel Plant-type Carbonic Anhydrase from Bacillus subtilis
Rishiram Ramanan,Krishnamurthi Kannan,Nadimuthu Vinayagamoorthy,Saravana Devi Sivanesan,Kunga Mohan Ramkumar,Tapan Chakrabarti 한국생물공학회 2009 Biotechnology and Bioprocess Engineering Vol.14 No.1
Carbonic anhydrase enzyme, one of the fastest known enzymes, remains largely unexplored in prokaryotes when compared to its mammalian counterparts despite its ubiquity. In this study, the enzyme has been purified from Bacillus subtilis SA3 using sequential Sephadex G-75 chromatography, DEAE cellulose chromatography, and sepharose-4B-L-tyrosine-sulphanilamide affinity chromatography and characterized to provide additional insights into its properties. The apparent molecular mass of carbonic anhydrase obtained by SDS-PAGE was found to be approximately 37 kDa. Isoelectric focusing of the purified enzyme revealed an isoelectric point (pI) of around 6.1 when compared with marker. The presence of metal ions such as Zn2+, Co2+, Cu2+, Fe3+, Mg2+, and anion SO4- increased enzyme activity while strong inhibition was observed in the presence of Hg2+, Cl-, HCO3-, and metal chelator EDTA. The optimum pH and temperature for the enzyme were found to be 8.3 and 37℃, respectively. Enzyme kinetics with p-nitrophenyl acetate as substrate at pH 8.3 and 37℃ determined the Vmax and Km values of the enzyme to be 714.28 μmol/mg protein/min and 9.09 mM, respectively. The Ki value for acetazolamide was 0.22 mM, compared to 0.099 mM for sulphanilamide. The results from N-terminal amino acid sequencing imply the purified protein is a putative beta-carbonic anhydrase with close similarities to CAs from plants, microorganisms.