Click for new scientific resources and news about Corona[COVID-19]

Paper Information

Journal:   IRANIAN JOURNAL OF PUBLIC HEALTH   AUGUST 2014 , Volume 43 , Number SUPPLEMENT 2; Page(s) 61 To 61.
 
Paper: 

NATIVE PAGE AS A TOOL FOR SEMIPURIFICATION OF CATALASE FROM KOCURIA ASB 107

 
 
Author(s):  NAJJARI MARYAM, MOOSAVI NEJAD ZAHRA, ASGARANI EZAT
 
* 
 
Abstract: 

Background: The aim of this study was the evaluation of possible potential of native polyacrylamide gel electrophoresis as a tool for partial purification of catalase from Kocuria ASB 107.
Methods: The bacterial culture was cultivated in TSB medium and then the biomass was collected within the stationary phase. The pellet was resuspend in 50 mM potassium phosphate buffer at pH 7 and washed for 5 times. The cells were lysed after 80min incubation in lysosyme solution at 37oC. The supernatant was isolated by centrifuge and catalase activity of the cell extract was checked by monitoring A240 in the presence of substrate (H2O2). Then the cell lysate was loaded on top of a native polyacrylamide gel (10%). Zymogram was obtained by adding diluted H2O2 on the gel surface. The band of catalase was cut and removed from the gel and check for catalase activity as mentioned above. The remained gel was stained by coomasie blue.
Results: Formation of oxygen bubbles on the gel indicated the precise location of catalase. Bands appeared in the remained gel after staining and destaining process.
Conclusion: According to our result we could observe catalase was partially purified among the mass of proteins in the cell extract as an individual bubble-forming bond on the gel.

 
Keyword(s): CATALASE, PURIFICATION, NATIVE PAGE, KOCURIA ASB 107
 
References: 
  • ندارد
 
  Yearly Visit 45
 
Latest on Blog
Enter SID Blog