Volume 10, Number 3 (yafte 2008)                   yafte 2008, 10(3): 13-19 | Back to browse issues page


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Halakhor S, Qujeq D, Shikhpour R. Determination of Sialyl trnsferase activity and effect of Phosphorylation and dephosphorylation Mechanisms. yafte. 2008; 10 (3) :13-19
URL: http://yafte.lums.ac.ir/article-1-85-en.html

Abstract:   (6654 Views)
Halakhor S1, Qujeq D2, Shikhpour R3 1. Instructor, Department of Biochemistry and Biophysics, Faculty of Medicine, Babol University of Medical Sciences, Babol, Iran 2. Associate professor, Department of Biochemistry and Biophysics, Faculty of Medicine, Babol University of Medical Sciences, Babol, Iran 3. GP, Babol, Iran Abstract Background: Previous reports show that phosphorylation anddephosphorylation mechanisms involve in regulation of sialyl transferaseactivity. The aim of this research was to study sialyl trnsferase activity with phosphorylation and dephosphorylation mechanisms. Materials and methods: This experimental trial study performed on 25 rats without signs of illness. Rat brains were pulled out and brain homogenization was done and then sialyl transferase purified purified from rat brain. Homogenization of rat brain is performed in the cephadex chromatography. We added protein kinaseokadaic acid and forbol to different groups. Data were statistically analyzed using SPSS soft wave. Results: Results showed a significant increase in sialyl transferase activity in the control group, comparing with protein kinase C and okadaic acid groups.Results showed a significant decrease in sialyl transferase activity incontrol group, comparing with protein phosphatase and forbol groups. Conclusion: Our findings show that sialyl transferase of rat brain with protein kinase decreases enzyme activity and these results were in accordance with other studies in this respect. We found that treatment of rat brain sialyl transferase by protein phosphatase increases its activity.
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Type of Study: Research |
Received: 2009/03/2

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