The glycation sensitivity was compared by incubating the purified lipid-free apoA-I (final 1 mg/mL) with 250 mM D-fructose (Sigma # F2793) in 200 mM potassium phosphate/0.02% sodium azide buffer (pH 7.4), as reported elsewhere [21 (link),37 (link)]. ApoA-I was incubated for up to 48 h in an atmosphere containing 5% CO2 at 37 °C. The extent of the advanced glycation reactions was determined by reading the fluorescence intensities at 370 nm (excitation) and 440 nm (emission), as described previously [56 (link)], using an FL6500 spectrofluorometer (Perkin-Elmer, Norwalk, CT, USA) with Spectrum FL software version 1.2.0.583 (Perkin–Elmer) and a 1 cm path-length Suprasil quartz cuvette (Fisher Scientific, Pittsburgh, PA, USA).
Suprasil quartz cuvette
Manufactured by Thermo Fisher Scientific
Sourced in United States
The Suprasil quartz cuvette is a laboratory equipment designed for spectroscopic analysis. It is made of high-quality quartz material that provides exceptional transparency across a wide range of wavelengths, enabling precise and reliable spectroscopic measurements.
Automatically generated - may contain errors
Lab products found in correlation
Fl6500 spectrofluorometer, by PerkinElmer (6 mentions)
Winlab software package 4, by PerkinElmer (5 mentions)
Ls55 spectrofluorometer, by PerkinElmer (5 mentions)
Spectrum fl software, by PerkinElmer (5 mentions)
D fructose, by Merck Group (1 mentions)
J 715 spectropolarimeter, by Jasco (1 mentions)
11 protocols using suprasil quartz cuvette
1
Glycation Sensitivity of Apolipoprotein A-I
2
Tryptophan Fluorescence in rHDL Nanoparticles
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Movement of tryptophan residues in the PCO-rHDL and SCWA-rHDL was determined from uncorrected spectra obtained on an LS55 spectrofluorometer (Perkin-Elmer, Norwalk, CT) and WinLab software package 4.00 (Perkin-Elmer) using a 1-cm path length Suprasil quartz cuvette (Fisher Scientific, Pittsburg, PA). The wavelengths of maximum fluorescence (WMF) in each rHDL were excited at 295 nm to avoid tyrosine fluorescence, and the emission spectra were scanned from 305 to 400 nm at room temperature.
3
Tryptophan Fluorescence Emission Spectra
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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.
4
Tryptophan Fluorescence in HDL3
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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.
5
Tryptophan Fluorescence in HDL3 with Ferrous Ions
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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)].
6
Tryptophan Fluorescence of ApoA-I
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The wavelengths of maximum fluorescence (WMF) of the tryptophan (Trp) residues in apoA-I were determined from the uncorrected spectra using an LS55 spectrofluorometer (Perkin-Elmer, Norwalk, CT, USA), as described previously [37 (link)], using WinLab software package 4.00 (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, and the emission spectra were scanned from 305 to 400 nm at room temperature [38 (link)]. For isothermal denaturation, the effects of urea addition on the secondary structures of Aβ and apoA-I in a lipid-bound state were monitored by measuring the α-helicity and tryptophan movement using CD and fluorospectroscopy, as reported elsewhere [36 (link),37 (link),38 (link)].
7
Tryptophan Fluorescence in HDL3
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The change in the secondary structure upon treatment with ferrous ion 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) 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. The emission spectra were scanned from 305 to 400 nm at room temperature.
8
Spectroscopic Analysis of Tryptophan Residues
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The wavelengths of maximum fluorescence (WMF) of the tryptophan (Trp) residues in apoA-I were determined from the uncorrected spectra using an LS55 spectrofluorometer (Perkin-Elmer, Norwalk, CT, USA), as described previously [42 (link)], using the WinLab software package 4.00 (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, and the emission spectra were scanned from 305 to 400 nm at room temperature [43 (link)]. For isothermal denaturation, the effects of urea addition on the secondary structures of SAA and apoA-I in a lipid-bound state were monitored by measuring the α-helicity and tryptophan movement by CD and fluorospectroscopy, as reported elsewhere [25 (link),33 (link)].
9
Protein Structural Changes in Lipid States
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The average alpha-helix content of proteins in lipid-free and lipid-bound states were measured by circular dichroism (CD) spectroscopy, using a J-715 Spectropolarimeter (Jasco, Japan). The spectra were obtained from 250-190 nm at 25°C in a 0.1-cm path-length quartz cuvette, using a 1.0-nm bandwidth, a speed of 50 nm/min, and a 4 s response time. The protein samples, which were dialyzed against the TBS to remove any residual fructose, of the lipid-free proteins were diluted to 0.07 mg/ml to avoid self-association of the apolipoproteins (Davidson et al., 1996 (link)), while lipid-bound proteins were diluted to 0.1 mg/ml. Four scans were accumulated and averaged. The α-helical content was calculated from the molar ellipticity at 222 nm (Chen et al., 1972 (link)).
The wavelengths of maximum fluorescence (WMF) of tryptophan residues in native and glycated apoA-I were determined from uncorrected spectra obtained on a LS55 spectrofluorometer (Perkin-Elmer, USA) using WinLab software package 4.00 (Perkin-Elmer) and a 1 cm path-length suprasil quartz cuvette (Fisher Scientific, USA). The samples were excited at 295 nm to avoid tyrosine fluorescence, and the emission spectra were scanned from 305–400 nm at room temperature.
The wavelengths of maximum fluorescence (WMF) of tryptophan residues in native and glycated apoA-I were determined from uncorrected spectra obtained on a LS55 spectrofluorometer (Perkin-Elmer, USA) using WinLab software package 4.00 (Perkin-Elmer) and a 1 cm path-length suprasil quartz cuvette (Fisher Scientific, USA). The samples were excited at 295 nm to avoid tyrosine fluorescence, and the emission spectra were scanned from 305–400 nm at room temperature.
10
Tryptophan Fluorescence Spectroscopy of apoA-I
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The wavelengths of maximum fluorescence (WMF) of the tryptophan (Trp) residues in apoA-I were determined from the uncorrected spectra using an LS55 spectrofluorometer (Perkin-Elmer, Norwalk, CT, USA), as described previously [54 (link)], using the WinLab software package 4.00 (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, and the emission spectra were scanned from 305 to 400 nm at room temperature [55 (link)]. For isothermal denaturation, the effects of urea addition on the secondary structures and apoA-I in a lipid-bound state were monitored by measuring tryptophan movement using fluorospectroscopy, as reported elsewhere [56 (link)].
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