Comparison of mitochondrial and cytosolic tRNA nucleotidyltransferases from Triticum aestivum

1999 ◽  
Vol 77 (2) ◽  
pp. 230-239
Author(s):  
Raffaela Vicaretti ◽  
Paul BM Joyce
Keyword(s):  
Triticum Aestivum ◽  
High Activity ◽  
Maximal Activity ◽  
Partial Purification ◽  
Elution Profile ◽  
Mitochondrial Enzyme ◽  
Alkaline Ph ◽  
Purification And Characterization ◽  
Purification Scheme

Here we report the partial purification and characterization of wheat mitochondrial ATP (CTP):tRNA nucleotidyltransferase (EC 2.7.7.25). Our purification scheme involves ammonium sulfate fractionation and chromatography on anion-exchange, hydroxyapatite, and affinity columns. Our results indicate that the enzyme is stable over a broad range of temperatures with highest activity at 37°C. High activity is seen at alkaline pH with a maximum at pH 9. The enzyme exhibits maximal activity in the presence of 10 mM MgCl2 and is inhibited by (at least) 100 mM NaCl. We also show that a second form of this enzyme exists in the wheat cytosolic fraction. This enzyme shares many features with the mitochondrial enzyme but differs from the mitochondrial enzyme in its elution profile from hydroxyapatite and in its response to manganese.Key words: tRNA nucleotidyltransferase, wheat, mitochondria.

scholarly journals Partial purification and characterization of xylanase from Bacillus cereus X3

2014 ◽  
Vol 11 (2) ◽  
pp. 1056-1061
Author(s):  
Baghdad Science Journal
Keyword(s):  
Bacillus Cereus ◽  
Maximal Activity ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Xylanase Production ◽  
Optimum Activity ◽  
Biology Department ◽  
Characterization Study ◽  
Quantitative Screening

Three strain of Bacillus cereus were obtained from soil sours Laboratories of Biology Department/ College of Science/ University of Baghdad. The bacteria secreted extracellular xylanase in liquid cultur the test ability of xylanase production from these isolates was studied semi quantitative and quantitative screening appeared that Bacillus cereus X3 was the highest xylanase producer. The enzyme was partial purification 191 fold from cultur by reached step by 4 U/mg proteins by ammonium sulfat precipitation 80%, Ion exchang DEAE-cellulos chromatography Characterization study of the partial purifation enzyme revealed that the enzyme had a optimum activity pH8 and activity was stable in the pH rang (8-10) for 30min. maximal activity was attained at 50C

scholarly journals Partial Purification and Characterization of Catalase from Banana Peels

2016 ◽  
Vol 13 (2) ◽  
pp. 392-398
Author(s):  
Baghdad Science Journal
Keyword(s):  
Gel Filtration ◽  
Maximum Velocity ◽  
Kinetic Studies ◽  
Maximal Activity ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Km Value ◽  
Almost All ◽  
Kinetics Of

Catalase (EC 1.11.1.6) is a well known enzyme which exists in almost all living creatures exposing to oxygen (such as plants, bacteria, and animals). It is a very necessary enzyme to protect the cell from oxidative detriment by reactive oxygen species (ROS). The aim of this study is the partial purification and characterization of Catalase enzyme from Banana peels. In this study, fresh banana peels are treated with 70 % ethanol ,further separated with chloroform ,water and ethyl acetate respectively .The supernatant of the enzymatic sample which is treated with chloroform is loaded into gel filtration column with Sephadex G-100 (1.0 x 90 cm) equilibrated with pH7 buffer media (phosphate buffer 0.1 M). Kinetic studies of the purified enzyme activity are measured and characterized .The maximal activity (26.04 units/mg) of catalase is observed with chloroform buffer extraction. The kinetics of catalase; Michalis constant Km and maximum velocity Vmax is determined using Linweaver- Burk plot, The Km value for catalase (434.7mM), Vmax (100 m mole min -1). Characterization results demonstrate that the optimal pH for activity is (7.6). And the optimal temperature for activity is 30?C .The present study indicates that Banana peels is a good source of catalase enzyme.

Partial Purification and Characterization of Protease from Germinating Wheat Seeds (Triticum aestivum L.)

2002 ◽  
Vol 5 (3) ◽  
pp. 317-320 ◽  
Author(s):  
Ranajit Kumar Shaha ◽  
N.K. Sana ◽  
N. Roy . ◽  
K.K. Biswas . ◽  
Abdullah Mamun
Keyword(s):  
Triticum Aestivum ◽  
Triticum Aestivum L ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Wheat Seeds

Purification and Characterization of a Bioscouring Pectate Lyase from Paenibacillus sp. WZ008 with High Activity on Pectin

2012 ◽  
Vol 441 ◽  
pp. 457-461
Author(s):  
Xiang Xian Ying ◽  
Li Na Chen ◽  
Mei Lan Yu ◽  
Qun Xue ◽  
Zhao Wang
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
High Activity ◽  
Culture Supernatant ◽  
Pectate Lyase ◽  
Maximal Activity ◽  
Polygalacturonic Acid ◽  
Purification And Characterization ◽  
Optimum Activity

An extracellular pectate lyase was purified from the culture supernatant of Paenibacillus sp. WZ008 grown in the pectin-containing medium. The enzyme was purified to homogeneity in three steps and found to have a molecular weight of around 45 kDa. Highly methylated pectin was the optimum substrate in the case of no Ca2+ addition while the enzyme exhibited the maximal activity on polygalacturonic acid in the presence of 4 mM Ca2+. The purified enzyme demonstrated the optimum activity at a temperature range of 55-60°C and pH 9.6. The Ca2+ ion enhanced the enzyme activity but Mn2+, Ba2+ and EDTA strongly inhibited it.

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