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Sunil Kumar,Santosh Dhillon,Dharam Singh,Randhir Singh 한국식품영양과학회 2004 Preventive Nutrition and Food Science Vol.9 No.3
Superoxide dismutase (SOD) from tomato (Lycopersicon esculentum Mill.) fruit was purified by ammonium sulphate precipitation, Sephadex G-100 and DEAE-cellulose column chromatographies. A 22 fold purification and an overall yield of 44% were achieved. The purified enzyme was a homodimer with Mr 37.1 kDa and subunit Mr 18.2 kDa as judged by SDS-PAGE. SOD showed K_m values of 25×10^(-6) M and 1.7×10^(-6) M for nitroblue tetrazolium (NBT) and riboflavin as substrates, respectively. The enzyme was thermostable upto 50℃ and exhibited pH optima of 7.8. The effect of metal ions and some other compounds on enzyme activity was studied. Co^(2+) and Mg^(2+) were found to enhance relative enzyme activities by 27% and 73%, respectively, while Mn^(2+) inhibited the SOD activity by 64%. However, Ca^(2+) and Cu^(2+) had no effect on enzyme activity. Other compounds like H₂O₂ and NaN₃ inhibited enzymatic activities by 60% and 32%, respectively, while sodium dodecyl sulphate (SDS), chloroform plus ethanol and β-mercaptoethanol had no effect on the activity of SOD.
Kumar, Sunil,Dhillon, Santosh,Singh, Dharam,Singh, Randhir The Korean Society of Food Science and Nutrition 2004 Preventive Nutrition and Food Science Vol.9 No.3
Superoxide dismutase (SOD) from tomato (Lycopersicon esculentum Mill.) fruit was purified by ammonium sulphate precipitation, Sephadex G-100 and DEAE-cellulose column chromatographies. A 22 fold purification and an overall yield of 44% were achieved. The purified enzyme was a homodimer with Mr 37.1 kDa and subunit Mr 18.2 kDa as judged by SDS-PAGE. SOD showed $K_{m}$ values of 25 ${\times}$ 10$^{-6}$ M and 1.7 ${\times}$ 10$^{-6}$ M for nitroblue tetrazolium (NBT) and riboflavin as substrates, respectively. The enzyme was thermostable upto 5$0^{\circ}C$ and exhibited pH optima of 7.8. The effect of metal ions and some other compounds on enzyme activity was studied. $Co^{2+}$ and $Mg^{2+}$ were found to enhance relative enzyme activities by 27 % and 73 %, respectively, while M $n^{2+}$ inhibited the SOD activity by 64%. However, $Ca^{2+}$ and C $u^{2+}$ had no effect on enzyme activity. Other compounds like $H_2O$$_2$ and Na $N_3$ inhibited enzymatic activities by 60% and 32%, respectively, while sodium dodecyl sulphate (SDS), chloroform plus ethanol and $\beta$-mercaptoethanol had no effect on the activity of SOD. of SOD.
( Matam Chandrasekharaiah ),( Appoothy Thulasi ),( M Bagath ),( Duvvuri Prasanna Kumar ),( Sunil Singh Santosh ),( Chenniappan Palanivel ),( Vazhakkala Lyju Jose ),( K. T. Sampath ) 생화학분자생물학회(구 한국생화학분자생물학회) 2011 BMB Reports Vol.44 No.1
Termites play an important role in the degradation of dead plant materials and have acquired endogenous and symbiotic cellulose digestion capabilities. The feruloyl esterase enzyme (FAE) gene amplified from the metagenomic DNA of Coptotermes formosanus gut was cloned in the TA cloning vector and subcloned into a pET32a expression vector. The Ft3-7 gene has 84% sequence identity with Clostridium saccharolyticum and shows amino acid sequence identity with predicted xylanase/chitin deacetylase and endo-1,4-beta-xylanase. The sequence analysis reveals that probably Ft3-7 could be a new gene and that its molecular mass was 18.5 kDa. The activity of the recombinant enzyme (Ft3-7) produced in Escherichia coli (E.coli) was 21.4 U with substrate ethyl ferulate and its specific activity was 24.6 U/mg protein. The optimum pH and temperature for enzyme activity were 7.0 and 37oC, respectively. The substrate utilization preferences and sequence similarity of the Ft3-7 place it in the type-D sub-class of FAE. [BMB reports 2011; 44(1): 52-57]