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

Please use this identifier to cite or link to this item: https://doi.org/10.1007/s10529-005-3894-z

Title:	An acid phosphatase from Manihot glaziovii as an alternative to alkaline phosphatase for molecular cloning experiments
Authors:	Tham, S.C. Lim, S.H. Yeoh, H.H.
Keywords:	Acid phosphatase Dephosphorylation Enzyme kinetics Manihot glaziovii
Issue Date:	Dec-2005
Citation:	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
URI:	http://scholarbank.nus.edu.sg/handle/10635/100049
ISSN:	01415492
DOI:	10.1007/s10529-005-3894-z
Appears in Collections:	Staff Publications

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