An acid phosphatase from Manihot glaziovii as an alternative to alkaline phosphatase for molecular cloning experiments
Tham, S.C. Lim, S.H. Yeoh, H.H.
Tham, S.C.
Lim, S.H.
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Alternative Title
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.
Keywords
Acid phosphatase, Dephosphorylation, Enzyme kinetics, Manihot glaziovii
Source Title
Biotechnology Letters
Publisher
Series/Report No.
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Date
2005-12
DOI
10.1007/s10529-005-3894-z
Type
Article