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Ryder, Alan G.; Glynn, Thomas J.; Przyjalgowski, Milosz; Szczupak, Bogusław

doi:10.1023/a:1016896314122

Cited by 23 publications

(10 citation statements)

References 6 publications

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“…Thus far, applications of diode laser-induced fluorescence detection in CE have been reported for wavelengths in the near-IR (785/780 nm), 1,2 red (635/670 nm), [3][4][5] green (532 nm) and InGaN-based violet (405 nm) regions. [6][7][8][9] Even though, only a few suitable labeling dyes are excited in these specific regions for all of the previously used diode lasers. 10 Light-emitting diodes (LEDs), developed since the 1960s, are exceptionally stable and intensive light sources.…”

Section: Introductionmentioning

confidence: 99%

UV Light-Emitting Diode-Induced Fluorescence Detection Combined with Online Sample Concentration Techniques for Capillary Electrophoresis

2006

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The application of an ultraviolet (UV) light-emitting diode (LED) to on-line sample concentration/fluorescence detection in capillary electrophoresis (CE) is described. The utility of a UV-LED (peak emission wavelength at 380 nm, ∼2 mW) for fluorescence detection was demonstrated by examining both a naturally fluorescent (riboflavin) compound and a nonfluorescent compound (tryptophan), respectively. The detection limit for riboflavin was determined to be 0.2 ppm by the normal MEKC mode, which was improved to 3 -7 ppb when dynamic pH-junction technique was applied. On the other hand, the detection limit of the tryptophan derivative was determined to be 1.5 ppm using the MEKC mode, which was improved to 3 ppb when the sweeping-MEKC mode was applied. In an analysis of an actual sample, the concentrations of riboflavin in beer, and tryptophan in urine and milk samples were determined, respectively.

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Section: Introductionmentioning

confidence: 99%

UV Light-Emitting Diode-Induced Fluorescence Detection Combined with Online Sample Concentration Techniques for Capillary Electrophoresis

2006

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“…3). The system, which was described previously, 37 has been modified to improve the accuracy of the lifetime measurement. In the earlier version of the DLFLM, a standard trinocular attachment (U-TR30, Olympus) was used in which the video port was used as the entry/exit for the laser excitation and fluorescence emission system.…”

Section: Methodsmentioning

confidence: 99%

Time-Resolved Fluorescence Microspectroscopy for Characterizing Crude Oils in Bulk and Hydrocarbon-Bearing Fluid Inclusions

et al. 2004

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Abstract:Time-resolved fluorescence data was collected from a series of 23 bulk crude petroleum oils and 6 microscopic Hydrocarbon-bearing Fluid Inclusions (HCFI). The data was collected using a Diode Laser Fluorescence Lifetime Microscope (DLFLM) over the 460-700 nm spectral range using a 405 nm excitation source. The correlation between intensity averaged lifetimes (τ ) and chemical and physical parameters was examined with a view to developing a quantitative model for predicting the gross chemical composition of hydrocarbon liquids trapped in HCFI. It was found that τ is nonlinearly correlated with the measured polar and corrected alkane concentrations, and that oils can be classified on this basis. However, these correlations all show a large degree of scatter, preventing accurate quantitative prediction of gross chemical composition of the oils. Other parameters such as API gravity and, asphaltene, aromatic, and sulphur concentrations do not correlate well with τ measurements. Individual HCFI were analysed using the DLFLM and time resolved fluorescence measurements were compared with τ data from the bulk oils. This enabled the fluid within the inclusions to be classified as either low alkane/high polar or high alkane/low polar. Within the high alkane/low polar group, it was possible to clearly discriminate HCFI from different locales and to see differences in the trapped hydrocarbon fluids from a single geological source. This methodology offers an alternative method for classifying the hydrocarbon content of HCFI, and observing small variations in the trapped fluid composition, that is less sensitive to fluctuations in the measurement method than fluorescence intensity based methods.

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“…A chambered coverglass with the dye sample is illuminated at sufficient laser power to achieve approximately 100,000 counts per second in the donor emission channel, and frame averaging is used to calibrate the software using the 2.5 ns reference sample. To verify the calibration, lifetime measurements are made of a second reference standard, 10 mM HPTS (8 -hydroxypyrene -1,3,6 -trisulfonic acid from Santa Cruz Biotechnology, Inc.) dissolved in phosphate buffer (PB) pH 7.8 (reference lifetime of 5.3 ns [13]). The distribution of the lifetimes for all the pixels in the image is determined using the phasor (polar) plot method [14][15][16][17][18][19].…”

Section: Fd Flim Measurementsmentioning

confidence: 99%

Measuring Protein Interactions Using Förster Resonance Energy Transfer and Fluorescence Lifetime Imaging Microscopy

Day

2014

Microsc Microanal

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The method of fluorescence lifetime imaging microscopy (FLIM) is a quantitative approach that can be used to detect Förster Resonance Energy Transfer (FRET). The use of FLIM to measure the FRET that results from the interactions between proteins labeled with fluorescent proteins (FPs) inside living cells provides a non-invasive method for mapping interactomes. Here, the use of the phasor plot method to analyze frequency domain (FD) FLIM measurements is described, and measurements obtained from cells producing the 'FRET standard' fusion proteins are used to validate the FLIM system for FRET measurements. The FLIM FRET approach is then used to measure both homologous and heterologous protein-protein interactions (PPI) involving the CCAAT/enhancer-binding protein alpha (C/EBPα). C/EBPα is a transcription factor that controls cell differentiation, and localizes to heterochromatin where it interacts with the heterochromatin protein 1 alpha (HP1α). The FLIM-FRET method is used to quantify the homologous interactions between the FP-labeled basic leucine zipper (BZip) domain of C/EBPα. Then the heterologous interactions between the C/EBPa BZip domain and HP1a are quantified using the FRET-FLIM method. The results demonstrate that the basic region and leucine zipper (BZip) domain of C/ EBPα is sufficient for the interaction with HP1α in regions of heterochromatin. Keywordsfluorescence lifetime imaging microscopy (FLIM); Förster resonance energy transfer (FRET) microscopy; fluorescent proteins (FPs); protein-protein interactions (PPI)

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Cited by 23 publications

References 6 publications

UV Light-Emitting Diode-Induced Fluorescence Detection Combined with Online Sample Concentration Techniques for Capillary Electrophoresis

UV Light-Emitting Diode-Induced Fluorescence Detection Combined with Online Sample Concentration Techniques for Capillary Electrophoresis

Time-Resolved Fluorescence Microspectroscopy for Characterizing Crude Oils in Bulk and Hydrocarbon-Bearing Fluid Inclusions

Measuring Protein Interactions Using Förster Resonance Energy Transfer and Fluorescence Lifetime Imaging Microscopy

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