An acid phosphatase from Manihot glaziovii as an alternative to alkaline phosphatase for molecular cloning experiments

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°C. It was inactivated at 65°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. © Springer 2005.