Isothermal titration calorimetric study on the binding of iron to human serum transferrin - experimental data

Experimental data for a paper entitled Calorimetric study on the effect of sialylation and synergistic anion on the binding of iron to human serum transferrin (paper in preparation; citing information will be updated pending publication). Separate files are provided for titrations of native (Tf+s) and desialylated (Tf-s) apotransferrin with FeNTA in the presence of carbonate and oxalate. Raw data with the corresponding fit results are available in .apj file format, which can be opened with MicroCal PEAQ-ITC Analysis software, available for download here: https://www.malvernpanalytical.com/en/support/product-support/microcal-range/microcal-itc-range/microcal-peaq-itc#software Raw data including control experiments are also included in ASCII (.csv) format. For more details, please visit: https://glymech.pharma.hr//GlyMech.html.This work was supported by funding from the Croatian Science Foundation grant UIP-2017-05-9537 – Glycosylation as a factor in the iron transport mechanism of human serum transferrin (GlyMech). Additional support was provided by the European Regional Development Fund grants for 'Strengthening of Scientific Research and Innovation Capacities of the Faculty of Pharmacy and Biochemistry at the University of Zagreb' (contract #KK.01.1.1.02.0021) and 'Development of methods for production and labelling of glycan standards for molecular diagnostics' (contract #KK.01.1.1.07.0055)