The catalytic activity of rHrGSTm1 was determined by water bath treatment at different temperatures (10 °C, 20 °C, 30 °C, 40 °C, 50 °C, 60 °C, 70 °C and 80 °C) for 15 min. Eight pH buffers (pH 6.0, 6.5, 7.0, 7.5, 8.0, 8.5 and 9.0) were used to detect the catalytic activity of rHrGSTm1, determined using phosphate buffers (100 mM) at pH 6.0, 6.5, 7.0, 7.5 and 8.0, and Tris hydrochloric acid buffers (100 mM) at pH 8.5 and 9.0. For the negative control, the denatured recombinant protein boiled for 7 min was used as the substrate. The experiment was repeated three times, and the highest enzyme activity was regarded as 100%.
Copyright and License information: The Author(s) ©2023 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
Do you have any questions about this protocol?
Post your question to gather feedback from the community. We will also invite the authors of this
article to respond.
Ask a
question
Post a Question
