RESUMO
Previous reports show that phosphorylation and dephosphorylation mechanisms involve in regulation of sialyl transferase activity. The aim of this research was to study sialyl transferase activity with phosphorylation and dephosphorylation mechanisms. 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 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 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 in control group, comparing with protein phosphatase and forbol groups. 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