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. 2017 Dec 21;7:18041. doi: 10.1038/s41598-017-18029-y

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© The Author(s) 2017

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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Construction scheme and characterization of palmitic acid-conjugated Uox-160AzF (a) Conjugation of Uox-160AzF and the palmitic acid analog containing an azide group (azide-Pal) via SPACC using a homo-bifunctional linker (DBCO-PEG4-DBCO) (b) The reaction mixture of Uox-160AzF and azide-Pal was further incubated with DBCO-Rho for fluorescence analysis. Fluorescence (Fluorescence Panel; excitation: 302 nm, emission: 510–610 nm) and Coomassie-stained image (Coomassie Panel) of protein gel of Uox-160AzF (lane 1) and Uox-160AzF reacted with DBCO-PEG4-DBCO linker (lane 2) taken by Bio-Rad ChemiDoc™ XRS+. M indicates a lane for molecular weight standards. (c) Enzymatic activity of Uox-160Pal relative to that of Uox-WT. Error bars represent standard deviations (n = 3). Enzymatic activity of Uox-160Pal was significantly reduced when compared to Uox-WT (two-tailed student’s t-test; *Indicates p < 0.01).