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Study of acid phosphatase in pea and tobacco
Šandová, Sandra ; Ryšlavá, Helena (advisor) ; Tichá, Marie (referee)
Phosphatases catalyze the hydrolytic fission of orthophosphoric acid ester. They are generally divided into acid and alkaline phosphatases according to their pH optimum. There was preparated the extract of leaves Nicotiana tabacum L. and Pissum sativum. Furthermore, there were determinated pea and tobacco phosphatases's rate constants. Reaction speed katalyzed by tobacco phosphatase is 10,0 mol/min.ml and by pea phosphatase 38,0 mol/min.ml using paraNP - phosphate as a substrate. Using a substrate phospho - L serine the reaction speed katalyzed by phosphatase of tobacco is 1,8 mol/min.ml and by phosphatase of pea is 0,4 mol/min.ml. Michaelis constant Km is 1,8 mM for tobacco phosphatase and 8,5 mM for pea phosphatase using paraNP - phosphate. Using a substrate phospho - L serine Michaelis constant Km of phosphatase of tobacco and pea is the same - 4,0 mM. The pH optimum of pea phosphatase is 5,0 using paraNP - phosphate as a substrate and 6,0 using phopho - L serine. pH optimum of tobacco phosphatase is 5,4 using paraNP - phosphate and 7,0 using phospho - L serine. Temperature optimum for pea phosphatase is 60 C and for tobacco phosphatase 55C.
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Study of acid phosphatase in pea and tobacco
Šandová, Sandra ; Ryšlavá, Helena (advisor) ; Tichá, Marie (referee)
Phosphatases catalyze the hydrolytic fission of orthophosphoric acid ester. They are generally divided into acid and alkaline phosphatases according to their pH optimum. There was preparated the extract of leaves Nicotiana tabacum L. and Pissum sativum. Furthermore, there were determinated pea and tobacco phosphatases's rate constants. Reaction speed katalyzed by tobacco phosphatase is 10,0 mol/min.ml and by pea phosphatase 38,0 mol/min.ml using paraNP - phosphate as a substrate. Using a substrate phospho - L serine the reaction speed katalyzed by phosphatase of tobacco is 1,8 mol/min.ml and by phosphatase of pea is 0,4 mol/min.ml. Michaelis constant Km is 1,8 mM for tobacco phosphatase and 8,5 mM for pea phosphatase using paraNP - phosphate. Using a substrate phospho - L serine Michaelis constant Km of phosphatase of tobacco and pea is the same - 4,0 mM. The pH optimum of pea phosphatase is 5,0 using paraNP - phosphate as a substrate and 6,0 using phopho - L serine. pH optimum of tobacco phosphatase is 5,4 using paraNP - phosphate and 7,0 using phospho - L serine. Temperature optimum for pea phosphatase is 60 C and for tobacco phosphatase 55C.
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