Abstract
An acid phosphatase, free of deoxyribonuclease activity, was isolated from Manihot glaziovii leaves. It had a Mr of 78 kDa and was optimally active at pH 4.3 and 52 degrees C. It was inactivated at 65 degrees C over 15 min. It had a broad substrate specificity with strongest activity towards p-nitrophenyl phosphate. The enzyme dephosphorylated linearized pUC18 DNA and preventing self-ligation under the same conditions used for calf intestine alkaline phosphatase.
MeSH terms
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Acid Phosphatase / chemistry
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Acid Phosphatase / isolation & purification
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Acid Phosphatase / metabolism*
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Alkaline Phosphatase / metabolism*
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Anions / pharmacology
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Cations, Divalent / pharmacology
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Cloning, Molecular / methods*
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Enzyme Stability
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Hydrogen-Ion Concentration
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Kinetics
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Manihot / enzymology*
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Molecular Weight
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Nitrophenols / metabolism
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Organophosphorus Compounds / metabolism
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Phosphorylation / drug effects
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Plant Leaves / enzymology
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Plasmids / genetics
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Plasmids / metabolism
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Reducing Agents / pharmacology
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Sodium Dodecyl Sulfate / pharmacology
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Substrate Specificity
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Temperature
Substances
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Anions
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Cations, Divalent
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Nitrophenols
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Organophosphorus Compounds
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Reducing Agents
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nitrophenylphosphate
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Sodium Dodecyl Sulfate
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Alkaline Phosphatase
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Acid Phosphatase