scholarly journals Characterization of Fructose-1,6-Bisphosphate Aldolase 1 of Echinococcus multilocularis

2021 ◽  
Vol 9 (1) ◽  
pp. 4
Author(s):  
Xuedong He ◽  
Jing Zhang ◽  
Yue Sun ◽  
Tianyan Lan ◽  
Xiaola Guo ◽  
...  

Glycolysis is one of the important ways by which Echinococcus multilocularis acquires energy. Fructose-1, 6-bisphosphate aldolase (FBA) plays an important role in this process, but it is not fully characterized in E. multilocularis yet. The results of genome-wide analysis showed that the Echinococcus species contained four fba genes (FBA1-4), all of which had the domain of FBA I and multiple conserved active sites. EmFBA1 was mainly located in the germinal layer and the posterior of the protoscolex. The enzyme activity of EmFBA1 was 67.42 U/mg with Km and Vmax of 1.75 mM and 0.5 mmol/min, respectively. EmFBA1 was only susceptible to Fe3+ but not to the other four ions (Na+, Ca2+, K+, Mg2+), and its enzyme activity was remarkably lost in the presence of 0.5 mM Fe3+. The current study reveals the biochemical characters of EmFBA1 and is informative for further investigation of its role in the glycolysis in E. multilocularis.

1979 ◽  
Vol 34 (3) ◽  
pp. 269-279 ◽  
Author(s):  
Sylvia Brabbs ◽  
J. R. Warr

SUMMARYFive clones of Chinese hamster ovary cells with increased resistance to bleomycin have been isolated following ethylmethanesulphonate mutagenesis. Resistance was stable in three of the clones, but unstable in the other two. One of the stably resistant clones was cross resistant to unrelated drugs, and in contrast to the parental cells, its response to bleomycin was potentiated by tween 80. These two observations suggested a membrane alteration in the resistant clone. There was no significant difference in bleomycin-inactivating enzyme activity between the parental and resistant clones.


PLoS ONE ◽  
2013 ◽  
Vol 8 (10) ◽  
pp. e75149 ◽  
Author(s):  
Sheng-Rui Liu ◽  
Wen-Yang Li ◽  
Dang Long ◽  
Chun-Gen Hu ◽  
Jin-Zhi Zhang

1980 ◽  
Vol 35 (3-4) ◽  
pp. 209-212 ◽  
Author(s):  
B. Schöbel ◽  
W. Pollmann

Abstract The isolation and characterization of a specific chlorogenic acid esterase is described. The enzyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means of ultrafiltration and column-chromatography. The pH- and temperature optimum were 6.5 and 45 °C respectively. Divalent cations were not required for the enzyme activity. As other esterases, this enzyme is inhibited by di-isopropyl-phosphorofluoridate. The Km-value is 0.70 mᴍ chlorogenic acid, the molecular weight 240000. The described enzyme is specific for chlorogenic acid. On the other hand a typical unspecific esterase like the pig liver esterases does not split chloro­genic acid. The isoelectric focusing reveals several isoenzymes of chlorogenase within a pI-range of 4.0-4.5.


2009 ◽  
Vol 10 (1) ◽  
pp. R5 ◽  
Author(s):  
Giselda Bucca ◽  
Emma Laing ◽  
Vassilis Mersinias ◽  
Nicholas Allenby ◽  
Douglas Hurd ◽  
...  

PLoS ONE ◽  
2016 ◽  
Vol 11 (4) ◽  
pp. e0151522 ◽  
Author(s):  
Parameswari Paul ◽  
Vignesh Dhandapani ◽  
Jana Jeevan Rameneni ◽  
Xiaonan Li ◽  
Ganesan Sivanandhan ◽  
...  

2016 ◽  
Vol 303 (1) ◽  
pp. 71-90 ◽  
Author(s):  
Ce Ma ◽  
Huping Zhang ◽  
Jiaming Li ◽  
Shutian Tao ◽  
Xin Qiao ◽  
...  

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