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. 2022 Apr 6;13:1870. doi: 10.1038/s41467-022-29512-0

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — a The citrullinated-rhGK was generated as described in Methods based on in vitro citrullination by PAD. The native and PAD treated-rhGK were subjected to electrophoresis and followed by immunoblot with anti-glucokinase (α-GK) and anti-citrulline (α-citrulline). b The catalytic activity was measured spectrophotometrically at 25 mM glucose on 1 µg of rhGK and PAD treated-rhGK, respectively (see Methods). The error bars indicated SD of mean. c Enzyme kinetic analysis of GK was measured with seven dilutions of glucose (0–50 mM) and analyzed using GraphPad Prism Software. Km and Vmax were calculated by rhGK and PAD-treated rhGK curves, respectively, with p value of 0.0093 (computed by the F-test) between two Michaelis–Menten equations.