Spectrum fl software

The primary sequence of EGF showed two Trp residues at the 49th and 50th amino acids in the C-terminal region. The Trp fluorescence was measured by determining the emission fluorescence maxima from the uncorrected spectra obtained on an FL6500 spectrofluorometer (Perkin-Elmer, Norwalk, CT, USA) using Spectrum FL software version 1.2.0.583 (Perkin-Elmer) using a 1 cm path-length Suprasil quartz cuvette (Fisher Scientific, Pittsburgh, PA, USA). The three equally diluted samples, i.e., Heberprot-P75^®, Easyef^®, and methyl-parabenzoic acid, were excited at 295 nm to avoid tyrosine fluorescence. The emission spectra were scanned from 190 to 900 nm at room temperature.

The change in the secondary structure upon treatment with OSO was observed at the wavelengths of maximum fluorescence (WMF) of the tryptophan residues in HDL₃. The WMF was determined from the uncorrected spectra obtained on an FL6500 spectrofluorometer (Perkin-Elmer, Norwalk, CT, USA) using Spectrum FL software version 1.2.0.583 (Perkin-Elmer) using a 1 cm path-length Suprasil quartz cuvette (Fisher Scientific, Pittsburgh, PA, USA). The samples were excited at 295 nm to avoid tyrosine fluorescence. The emission spectra were scanned from 305 to 400 nm at room temperature.

The change in secondary structure upon treatment with ferrous ions was observed at the WMF of the tryptophan residues in HDL₃. The WMF was determined from the uncorrected spectra obtained on an FL6500 spectrofluorometer (Perkin–Elmer, Norwalk, CT, USA) using Spectrum FL software version 1.2.0.583 (Perkin–Elmer) and a 1 cm path-length Suprasil quartz cuvette (Fisher Scientific, Pittsburgh, PA, USA). The samples were excited at 295 nm to avoid tyrosine fluorescence. As described previously, the emission spectra were scanned from 305 to 400 nm at room temperature [56 (link)].