Please use this identifier to cite or link to this item:
|Title:||Development of an UPLC-MS/MS method for assaying the enzymatic activity of propionyl coenzyme-A carboxylase||Authors:||Damavandi, M.D.
|Issue Date:||Feb-2014||Citation:||Damavandi, M.D., Chan, E.C.Y., Kraus, J.P., Ho, P.C.-L., Kang, T.S. (2014-02). Development of an UPLC-MS/MS method for assaying the enzymatic activity of propionyl coenzyme-A carboxylase. Bioanalysis 6 (3) : 335-348. ScholarBank@NUS Repository. https://doi.org/10.4155/bio.13.297||Abstract:||Background: Propionyl coenzyme-A carboxylase (PCC) is a mitochondrial enzyme previously quantifiable only by radiometric assay. Herein, we report a UPLC-MS/MS method as a superior alternative method for assaying PCC's activity. Methodology & Results: For the development of the UPLC-MS/MS method, the mass spectra of propionyl coenzyme-A and methyl malonyl coenzyme-A precursor ions, and their full scan product ions were determined. MRM was used for the quantification of the analytes. The method showed good linearity and selectivity for further bioanalytical study. Conclusion: The developed UPLC-MS/MS method is capable of rapidly quantifying PCC's enzymatic activity and demonstrated suitability for assaying PCC's activity in complex biological samples. Thus, the method will be useful in validating recombinant expression of PCC, and potentially for routine quantification of mitochondrial PCC's activity level in patient cells. © 2014 Future Science Ltd.||Source Title:||Bioanalysis||URI:||http://scholarbank.nus.edu.sg/handle/10635/105828||ISSN:||17576180||DOI:||10.4155/bio.13.297|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Nov 21, 2019
WEB OF SCIENCETM
checked on Nov 13, 2019
checked on Nov 9, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.