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. 2020 Feb 3;25(3):645. doi: 10.3390/molecules25030645

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© 2020 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 (http://creativecommons.org/licenses/by/4.0/).

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In vitro characterization of fragment GAL-012. (A) GAL-012 (orange) docked into GALT. (B) Chemical structure of fragment GAL-012. (C) Lineweaver-Burke plot of GALT reaction velocities as measured in varying concentrations of GAL-012. (D) SDS-PAGE of selected purified recombinant enzymes (M: Molecular weight marker; 1: Purified GALT; 2: Purified GALE; 3: Purified UGDH; 4: Purified UGP2; 5: Purified AGX1/UAP1.) (E) Reaction mechanisms of selected enzymes—GALT, UGP2, AGX1/UAP1, UGDH, GALE.

In vitro characterization of fragment GAL-012. (A) GAL-012 (orange) docked into GALT. (B) Chemical structure of fragment GAL-012. (C) Lineweaver-Burke plot of GALT reaction velocities as measured in varying concentrations of GAL-012. (D) SDS-PAGE of selected purified recombinant enzymes (M: Molecular weight marker; 1: Purified GALT; 2: Purified GALE; 3: Purified UGDH; 4: Purified UGP2; 5: Purified AGX1/UAP1.) (E) Reaction mechanisms of selected enzymes—GALT, UGP2, AGX1/UAP1, UGDH, GALE.