Please use this identifier to cite or link to this item:
|Title:||An acid phosphatase from Manihot glaziovii as an alternative to alkaline phosphatase for molecular cloning experiments|
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
WEB OF SCIENCETM
checked on Feb 19, 2019
checked on Jan 18, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.