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. 2022 Dec 29;24(1):559. doi: 10.3390/ijms24010559

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Enzyme activity and thermal stability of purified ASNS proteins. (A) ASNS mRNA levels in non-transfected HEK293T cells and in HEK293T-based cell lines stable-expressing WT, N80S, or S480F ASNS variants. The mRNA content was detected by qRT-PCR, normalized to GAPDH mRNA, and plotted relative to WT. (B) Immunoblot for each of the ASNS variant proteins. GAPDH protein served as the loading control. (C) Enzyme activity of purified WT, N80S, and S480F ASNS proteins. A reaction with no protein added serves as a negative control to show background detection. The data are the averages ± standard deviations of assays in triplicate, and an asterisk indicates that the value is statistically different from the WT with a p-value of ≤0.05. (D) The melting points of purified WT, N80S, and S480F proteins as detected by differential scanning fluorimetry.