Issue 71, 2021
From the journal:

Chemical Communications

A novel ratiometric MALDI-MS quantitation strategy for alkaline phosphatase activity with a homogeneous reaction and a tunable dynamic range†

Rong-Na Ma, ORCID logo ‡*a   Min Zhang,‡a   Chao-Long Hu,a   Hui-Jing Pan,a   Lei Sib  and  Huaisheng Wang ORCID logo *a  

* Corresponding authors

a School of Chemistry and Chemical Engineering, Shandong Provincial Key Laboratory/Collaborative Innovation Center of Chemical Energy Storage, Liaocheng University, Liaocheng 252059, Shandong, P. R. China
E-mail: marongna@lcu.edu.cn, hswang@lcu.edu.cn

b Department of Clinical Laboratory, Liaocheng People's Hospital, Shandong First Medical University, Liaocheng 252000, Shandong, P. R. China

Abstract

A unique ratiometric MALDI-MS strategy is proposed for the convenient and reliable quantitation of alkaline phosphatase based on the homogeneous enzymatic cleavage of a coded phosphopeptide (CPP)-triggered double-signal output. The dynamic range can be tuned by simply adjusting the primary concentration of CPP. The proposed strategy is also capable of being challenged by real human serum, and thus it may offer a wonderful approach for the convenient identification and quantitation of various enzyme activities in clinical diagnosis.

Graphical abstract: A novel ratiometric MALDI-MS quantitation strategy for alkaline phosphatase activity with a homogeneous reaction and a tunable dynamic range

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Article information

DOI
https://doi.org/10.1039/D1CC03863J
Article type
Communication
Submitted
16 Jul 2021
Accepted
05 Aug 2021
First published
18 Aug 2021

Chem. Commun., 2021,57, 8885-8888

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A novel ratiometric MALDI-MS quantitation strategy for alkaline phosphatase activity with a homogeneous reaction and a tunable dynamic range

R. Ma, M. Zhang, C. Hu, H. Pan, L. Si and H. Wang, Chem. Commun., 2021, 57, 8885 DOI: 10.1039/D1CC03863J

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