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|Title:||An acid phosphatase from Manihot glaziovii as an alternative to alkaline phosphatase for molecular cloning experiments|
|Source:||Tham, S.C., Lim, S.H., Yeoh, H.H. (2005-12). An acid phosphatase from Manihot glaziovii as an alternative to alkaline phosphatase for molecular cloning experiments. Biotechnology Letters 27 (23-24) : 1865-1868. ScholarBank@NUS Repository. https://doi.org/10.1007/s10529-005-3894-z|
|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.|
|Source Title:||Biotechnology Letters|
|Appears in Collections:||Staff Publications|
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