The data presented in Figs describe the

The data presented in Figs. 1–9 describe the standardization of enzyme and analytes. Reaction progress curve data is provided for experiments evaluating the effects of variable substrate concentration (Figs. 10–13, [Myr] = 8.83Uml−1), variable enzyme concentration (Fig. 14), variable STA-9090 (Figs. 15–18, [Myr] = 8.83Uml−1; Figs. 19–21, [Myr] = 1.77Uml−1), and variable temperature (Figs. 22–25, [Myr] = 7.06Uml−1; Figs. 26–28, [Myr] = 1.77Uml−1). Reaction progress curve data was fit to the modified Lambert W(x) using nonlinear regression [1]. Initial rates were independently obtained from progress curves tracking analyte ([Gluc]t, [ITC]t, or [nitrile]t) at a specific wavelength, then normalized for the concentration of myrosinase (V0 [Myr]−1, min−1) [1]. Complete original datasets for each figure are provided as Supplementary material.
Experimental design,materials and methods
Acknowledgements We would like to extend our thanks to Brandon Gustafson, the faculty and staff in the Department of Chemistry at Augustana University, and the Mass Spectrometry & Analytical Proteomics Laboratory at the University of Kansas. This research was supported by an Institutional Development Award (IDeA) from the National Institute of General Medical Sciences of the National Institutes of Health under grant number P20GM103443. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. This research was also supported by a Research Infrastructure Improvement (RII) Track-1 award to South Dakota Experimental Program to Stimulate Competitive Research (SD EPSCoR) from the National Science Foundation and the state of South Dakota, under grant number IIA-1355423. Funding was also provided by the Augustana Research and Artist Fund (ARAF), and Augustana University.
Data Genotype and allele distribution for polymorphisms T786C and G894T in patients and controls are presented in Tables 1 and 2 respectively. No statistically significant differences were obtained [1]. eNOS mRNA levels normalized to GAPDH are presented in Fig. 1 (Sickle Cell Disease patients relative to controls) and Fig. 2 (patients of eNOS 786TC and CC genotypes relative to patients of TT genotype).
Experimental design, materials and methods
Acknowledgments The study was supported by the Program: “IKY fellowships of excellence for postgraduate studies in Greece-Siemens Program”.
Data Urinary metabolites detected in 10 normal, healthy human urine samples from fasting subjects were collected from two different 1H NMR magnets (600 and 700MHz). Pearson correlation coefficient was estimated for 151 metabolites that were selected based on their known presence in human urine samples [2,3]. A total of 57 metabolites (38%) were detected on both 600 and 700MHz systems that had a strong R2 of >0.7, listed in Supplementary Table 1. A bias of >0.5 was present in 7 additional samples, based on slope linearity of each metabolite, with a final total of 50 metabolites (33%) could be reproducibly detected on the 2 different NMR magnets within the same 10 urine samples.
Experimental design, materials and methods
Acknowledgments The work described here was supported by a grant from OHS Futures, Government of Alberta.
Data HepG2 cells were transfected with the plasmids: pcENS1, pcDNA3 and pMAXGFP. To produce accurate data, we used three independent experimental biological replicates and samples were submitted to LTQ-Orbitrap XL (Thermo Scientific). Data analysis, using the PatternLab for Proteomics software, identified 14,138 peptides which mapped to 4756 proteins, from all conditions (HepG2 transfected with the three different plasmids and non-transfected cells) (Supplementary Table S1a–h). Applying the maximum parsimony principle we found 2314 proteins (Supplementary Table S1g). Using the Tfold module we generate the differential abundance distribution when comparing: non-transfected HepG2 x cell transfected with pcDNA3 (Table 1); HepG2 transfected with pcDNA3 x pcENS1 (Table 2) and cells transfected with pMAGFP x pcENS1 (Table 3)[1].