Relevant bibliographies by topics / Lambda fluorescent

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Academic literature on the topic 'Lambda fluorescent'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Lambda fluorescent"

1

Voss, H., J. Zimmermann, C. Schwager, H. Erfle, J. Stegemann, K. Stucky, and W. Ansorge. "Automated fluorescent sequencing of lambda DNA." Nucleic Acids Research 18, no. 17 (1990): 5314. http://dx.doi.org/10.1093/nar/18.17.5314.

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Lallement, Pierre-Alexandre, Edgar Meux, José M. Gualberto, Pascalita Prosper, Claude Didierjean, Frederick Saul, Ahmed Haouz, Nicolas Rouhier, and Arnaud Hecker. "Structural and enzymatic insights into Lambda glutathione transferases from Populus trichocarpa, monomeric enzymes constituting an early divergent class specific to terrestrial plants." Biochemical Journal 462, no. 1 (July 24, 2014): 39–52. http://dx.doi.org/10.1042/bj20140390.

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The resolution of Lambda GST crystal structures in complex with glutathione and competition experiments with fluorescent probes reveal that poplar Lambda GSTs are involved in the reduction of glutathionylated substrates.
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3

Wu, Tongbo, Xianjin Xiao, Feidan Gu, and Meiping Zhao. "Sensitive discrimination of stable mismatched base pairs by an abasic site modified fluorescent probe and lambda exonuclease." Chemical Communications 51, no. 98 (2015): 17402–5. http://dx.doi.org/10.1039/c5cc05749c.

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An abasic site modified fluorescent probe has been developed which enabled the rapid discrimination of stable single mismatched base pairs by lambda exonuclease with remarkably high discrimination factors (447 for T:G and 238 for A:G).
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4

Chen, F. T., and R. A. Evangelista. "Feasibility studies for simultaneous immunochemical multianalyte drug assay by capillary electrophoresis with laser-induced fluorescence." Clinical Chemistry 40, no. 9 (September 1, 1994): 1819–22. http://dx.doi.org/10.1093/clinchem/40.9.1819.

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Abstract We present a method for the simultaneous quantification of multiple drug analytes in urine, based on combining immunochemical binding with capillary electrophoretic separation. Two fluorescent drug-cyanine (Cy) dye conjugates were prepared as competing species for the immunoassay. Morphine was derivatized with Cy5 (lambda max = 652 nm, epsilon = 215,000 mol-1cm-1 L), phencyclidine (PCP) with Cy5.5 (lambda max = 675 nm, epsilon = 200,000 mol-1cm-1L). The high-efficiency resolving power of the capillary electrophoresis system (20 microns x 27 cm column) separated the individual labeled drugs, and the antigen-antibody complexes were detected by laser-induced fluorescence (laser: 10 mW He-Ne at 632.8 nm) with Cy5 diacid as internal standard. Simultaneous competitive immunoassay of morphine and PCP in urine showed that the free labeled-drug peak areas were proportional to the concentrations of the drug species present in the urine sample. This immunoassay can be performed routinely and reproducibly in < 5 min with analytical detection limits of 4 nmol/L for PCP and 40 nmol/L for morphine.
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Smith, David L., Douglas K. Struck, J. Martin Scholtz, and Ry Young. "Purification and Biochemical Characterization of the Lambda Holin." Journal of Bacteriology 180, no. 9 (May 1, 1998): 2531–40. http://dx.doi.org/10.1128/jb.180.9.2531-2540.1998.

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ABSTRACT Holins are small phage-encoded cytoplasmic membrane proteins, remarkable for their ability to make membranes permeable in a temporally regulated manner. The purification of S105, the λ holin, and one of the two products of gene S is described. Because the wild-type S105 holin could be only partially purified from membrane extracts by ion-exchange chromatography, an oligohistidine tag was added internally to the S105 sequence for use in immobilized metal affinity chromatography. An acceptable site for the tag was found between residues 94 and 95 in the highly charged C-terminal domain of S. This allele, designated S105H94, had normal lysis timing under physiological expression conditions. The S105H94 protein was overproduced, purified, and characterized by circular dichroism spectroscopy, which revealed approximately 40% alpha-helix conformation, consistent with the presence of two transmembrane helices. The purified protein was then used to achieve release of fluorescent dye loaded in liposomes in vitro, whereas protein from an isogenic construct carrying an S mutation known to abolish hole formation was inactive in this assay. These results suggest that S is a bitopic membrane protein capable of forming aqueous holes in bilayers.
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Gillen, C. M., A. Takamata, G. W. Mack, and E. R. Nadel. "Measurement of plasma volume in rats with use of fluorescent-labeled albumin molecules." Journal of Applied Physiology 76, no. 1 (January 1, 1994): 485–89. http://dx.doi.org/10.1152/jappl.1994.76.1.485.

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We describe a method for measuring plasma volume (PV) in small animals that allows small sample sizes but does not require the use of radioisotopes and thus is a convenient approach for making repeated measurements. Texas Red covalently bound to albumin (TR-A) was used in a typical indicator-dilution technique to measure PV. The relative fluorescent intensity of TR-A is linear to its concentration (up to 0.15 mg/ml) at an excitation lambda of 590 nm and an emission lambda of 610 nm. Catheters were inserted through the right jugular vein of anesthetized rats and threaded into the vena cava. A 0.5-ml control blood sample was taken, a measured quantity of TR-A was injected, and the catheter was flushed with saline. A 0.5-ml postinjection sample was taken 5 min after TR-A injection. PV was calculated by comparing the difference between the relative fluorescent intensity of control and postinjection plasma samples to a standard. The PV of 22 rats [362 +/- 14 (SE) g] was 14.1 +/- 0.4 ml (39.6 +/- 0.9 ml/kg body wt) measured by the TR-A method and 12.8 +/- 0.4 ml (35.9 +/- 1.0 ml/kg body wt) measured by a standard radioiodinated albumin method. There was a strong correlation between PV measured by both methods in the same rat (r = 0.90, P < 0.01). Infusion experiments indicated that the TR-A method can detect acute changes in PV, and repeated measurements of PV made on a chronically instrumented rat demonstrated that the method can reliably measure PV on consecutive days.
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Xi, He, Yang Liu, Chun-Xue Yuan, Ye-Xin Li, Lei Wang, Xu-Tang Tao, Xiao-Hua Ma, Chun-Fu Zhang, and Yue Hao. "Through space charge-transfer emission in lambda (Λ)-shaped triarylboranes and the use in fluorescent sensing for fluoride and cyanide ions." RSC Advances 5, no. 57 (2015): 45668–78. http://dx.doi.org/10.1039/c5ra07912h.

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By introducing a twisted and non-conjugated Λ-shaped TB scaffold to triarylboranes, we provide an efficient strategy to develop a new class of organoboron compounds applied as colorimetric and ratiometric fluorescent sensors for fluoride and cyanide.
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Ioannou, P. C., and D. G. Konstantianos. "Fluorometric determination of magnesium in serum with 2-hydroxy-1-naphthaldehyde salicyloylhydrazone." Clinical Chemistry 35, no. 7 (July 1, 1989): 1492–96. http://dx.doi.org/10.1093/clinchem/35.7.1492.

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Abstract This simple, rapid, sensitive fluorometric method for determining magnesium is based on formation of a fluorescent complex of magnesium with 2-hydroxy-1-naphthaldehyde salicyloyl-hydrazone in alkaline ethanolic medium (lambda ex = 420 nm, lambda em = 460 nm). The detection limit of the method is 0.05 microgram/L (2 nmol/L) and the relative standard deviations (CVs) are 0.8%, 1.1%, and 2.5% at magnesium concentrations of 50, 5.0, and 0.50 microgram/L, respectively. The standard curve is linear from 0 to 250 micrograms/L (0-10 mumol/L). We investigated the chemistry of the reaction, and have applied the method to determine magnesium in 100-fold-diluted, otherwise untreated serum samples. Within-run CVs for the method were 1.7%, 1.1%, and 1.3% at mean magnesium concentrations of 15.7, 26.4, and 36.2 mg/L, respectively. Day-to-day CVs were 2.7%, and 3.6% at mean magnesium concentrations of 10.1 and 25.5 mg/L, respectively. Samples from 96 hospitalized patients in intensive-care units were analyzed by the proposed method (y) and by an automated colorimetric method involving Magon sulfonate reagent (x). Linear regression analysis of the results yielded: y = 1.01x - 0.04 (r = 0.982, Sxy = 0.90).
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9

Newmeyer, D. D., D. R. Finlay, and D. J. Forbes. "In vitro transport of a fluorescent nuclear protein and exclusion of non-nuclear proteins." Journal of Cell Biology 103, no. 6 (December 1, 1986): 2091–102. http://dx.doi.org/10.1083/jcb.103.6.2091.

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An in vitro system was developed that provides a quick microscopic assay for nuclear transport. The assay uses an extract of Xenopus eggs, normal or synthetic nuclei, and a fluorescently labeled nuclear protein, nucleoplasmin. This in vitro system accurately mimics in vivo nuclear transport, both in exclusivity and in the amount of accumulation observed (up to 17-fold). Selective accumulation of fluorescent nucleoplasmin is observed microscopically within 30 min with rat liver nuclei, Xenopus embryonic nuclei, regrown Xenopus sperm nuclei, or nuclei reconstituted in vitro from bacteriophage lambda DNA. This transport requires the signal domain of nucleoplasmin. Furthermore, the ability of nuclei to accumulate nucleoplasmin directly correlates with their ability to exclude the fluorescent non-nuclear proteins, FITC-immunoglobulin and phycoerythrin. An active transport model would predict that nuclear transport be temperature- and energy-dependent and that inhibition of transport by either low temperature or energy depletion would be reversible. Both predictions were confirmed in our system. Nucleoplasmin accumulation increases with temperature, while the protein is completely excluded at 0 degrees C. The effects of low temperature are reversible. As found for 125I-labeled nucleoplasmin (Newmeyer, D. D., J. M. Lucocq, T. R. Bürglin, and E. M. De Robertis, 1986, EMBO (Eur. Mol. Biol. Organ.) J., 5:501-510), transport of fluorescent nucleoplasmin is inhibited by ATP depletion. This effect is reversed by later ATP addition. Under ATP-depleted conditions non-nuclear proteins continue to be excluded. These results argue for a direct role of ATP in transport rather than for a simple role in preserving envelope integrity. In a first step towards defining the minimum requirements for a transport medium, egg extracts were depleted of membrane vesicles. Membrane-depleted extracts neither support transport nor maintain the integrity of the nuclear envelope.
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Bailey, G. G., and L. L. Needham. "Simultaneous quantification of erythrocyte zinc protoporphyrin and protoporphyrin IX by liquid chromatography." Clinical Chemistry 32, no. 12 (December 1, 1986): 2137–42. http://dx.doi.org/10.1093/clinchem/32.12.2137.

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Abstract A simple, rapid, specific, and sensitive isocratic "high-performance" liquid-chromatographic procedure is described for measuring protoporphyrin (PPIX) and zinc protoporphyrin (ZPP) in erythrocytes. A 30-microL whole-blood sample is treated with a solution of formic acid, deproteinized with acetone, and centrifuged. A 20-microL aliquot of the supernate is injected into a system consisting of a stationary phase of mu-Bondapak C18 and a mobile phase of acetone, methanol, water, and formic acid. ZPP and PPIX are detected fluorometrically (lambda ex = 417 nm, lambda em = 635 nm) within 6 min. The range of linearity extends beyond 10 mg/L for ZPP and 580 micrograms/L for PPIX. The detection limits for ZPP and PPIX are 11.9 micrograms/L (6.93 pg) and 2.55 micrograms/L (1.485 pg), respectively. The precision for ZPP and PPIX determinations averaged 2.86 and 5.59%, respectively, for within-day CVs and 4.98 and 8.14, respectively, for among-day CVs. Analytical recoveries averaged 97.2% for ZPP and 101.5% for PPIX. Interferences in the form of fluorescent quenching of ZPP and PPIX by hemin are avoided by chromatographic separation. We also used this method to determine the purity of commercially prepared ZPP, and compared the results obtained with this method with those from an extraction method.
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Dissertations / Theses on the topic "Lambda fluorescent"

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Alvarez, Sanchez Luis Javier. "Dynamique de propagation de bactériophages." Paris 6, 2007. http://www.theses.fr/2007PA066180.

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Nous avons réalisé une étude centrée sur la propagation virale du bactériophage lambda. Afin de caractériser en détail la dynamique de formations des plaques, nous avons génétiquement modifié le phage lambda de façon à rendre sa capside fluorescente en créant une fusion entre la protéine GpD de la capside du phage et la protéine EYFP. Le comportement de ce phage modifié a été caractérisé et son coefficient de diffusion au sein d’une plaque a été mesuré avec la technique de FRAPP. Ensuite nous avons étudié les profiles de population de phages au sein dúne plaque avec la technique de vidéomicroscopie en time-lapse. Des expériences supplémentaires en time-lapse ont été réalisées afin de caractériser la croissance des bactéries hôte en boîte de Petri sur un substrat d’agar. Les résultats de propagation obtenus sont comparés avec les modèles et expériences antérieurs développés afin de décrire la propagation du phage T7. Pour finir, nous avons réalisé des simulations numériques complémentaires qui sont qualitativement en accord avec les résultats expérimentaux
We have developed a study focused on the viral propagation of the lambda bacteriophage. With the purpose of a detailed characterization of the dynamics of the spread of infection during the formation of plaques, we have constructed a bacteriophage lambda carrying a fluorescent fusion between the minor protein of the capsid GpD and the Enhanced Yellow Fluorescent Protein (EYFP). The next step has been to perform the preliminary characterisation of the properties of this new fluorescent virus including measurements of its diffusion coefficient on a plaque using the technique called FRAPP. Subsequently we have measured the dynamic of the phage population profiles in time within the plaque using time-lapse videomicroscopy. Supplementary experiments have been done in order to characterize the bacterial growth in Petri dishes on an agar substrate. The results have been compared to previous experiments and theoretical works performed in order to describe the propagation of the T7 bacteriophage. Finally, we have performed complementary numerical simulations that are in qualitative agreement with the experimental results
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Ghozzi, Stéphane. "Dynamique d'Expression d'un Réseau de Régulation Génétique : la Décision Lyse/Lysogénie chez le Bactériophage Lambda." Phd thesis, Université Pierre et Marie Curie - Paris VI, 2009. http://tel.archives-ouvertes.fr/tel-00515109.

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Lors d'une infection par le virus Lambda, une bactérie peut suivre l'une ou l'autre de deux voies très différentes : la lyse, où le virus se multiplie, tue l'hôte et est relâché dans l'environnement, ou la lysogénie, où l'ADN viral est intégré dans le chromosome de l'hôte et celui-ci devient immunisé à une surinfection. La "décision" entre la lyse et la lysogénie est prise aléatoirement, mais les probabilités de suivre chacune des deux voies dépend du nombre de virus infectant la cellule en même temps et de son état physiologique : un faible nombre de virus par bactérie, un milieu riche ou des cellules en phase de croissance exponentielle favorisent la lyse, alors que les conditions opposées favorisent la lysogénie. Cela est rendu possible par un ensemble de cinq gènes, sous quatre promoteurs, interagissant les uns avec les autres et avec des protéines de l'hôte. Des paires de gènes codant pour des protéines fluorescentes ont été insérés dans le génome de Lambda. En mesurant les niveaux de fluorescence de bactéries individuelles, nous pouvons déterminer, au cours de la décision, les taux d'expression de gènes de ce réseau et leurs corrélations deux à deux. En variant systématiquement les conditions de croissance, nous pouvons ainsi obtenir une description riche de la dynamique, notamment du rôle du bruit stochastique et de son contrôle, de ce réseau de régulation naturel. Enfin, nous avons complété un programme informatique développé au laboratoire de façon à pouvoir comparer le réseau de Lambda à des réseaux générés sur ordinateur et ayant le même comportement. Cela aidera à mieux comprendre la structure particulière de ce réseau.
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Neuhaus, Jochen, Birgit Schröppel, Martin Dass, Hans Zimmermann, Hartwig Wolburg, Petra Fallier-Becker, Thomas Gevaert, Claus J. Burkhardt, Do Hoang Minh, and Jens-Uwe Stolzenburg. "3D-electron microscopic characterization of interstitial cells in the human bladder upper lamina propria." Universitätsklinikum Leipzig, 2017. https://ul.qucosa.de/id/qucosa%3A15544.

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1) Aims To explore the ultrastructure of interstitial cells in the upper lamina propria of the human bladder, to describe the spatial relationships and to investigate cell-cell contacts. 2) Methods Focused ion beam scanning electron microscopy (FIB-SEM), 3-View SEM and confocal laser scanning microscopy were used to analyze the 3D ultrastructure of the upper lamina propria in male and female human bladders. 3) Results 3View-SEM image stacks as large as 59µm x 59µm x 17µm (xyz) at a resolution of 16nm x 16nm x 50 nm and high resolution (5nm x 5nm x 10nm) FIB-SEM stacks could be analyzed. Interstitial cells with myoid differentiation (mIC) and fibroblast like interstitial cells (fIC) were the major cell types in the upper lamina propria. The flat, sheet-like ICs were oriented strictly parallel to the urothelium sheet-like morphology. No spindle shaped cells were present. We furthermore identified one branched cell (bIC) with several processes contacting urothelial cells by penetrating the basal membrane. This cell did not make any contacts to other ICs within the upper lamina propria. We found no evidence for the occurrence of telocytes in the upper lamina propria. 4) Conclusions Comprehensive 3D-ultrastructural analysis of the human bladder confirmed distinct subtypes of interstitial cells. We provide evidence for a foremost unknown direct connection between a branched interstitial cell and urothelial cells of which the functional role has still to be elucidated. 3D-ultrastructure analyses at high resolution are needed to further define the subpopulations of lamina propria cells and cell-cell interactions.
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Books on the topic "Lambda fluorescent"

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United States. Environmental Protection Agency. WSTB., ed. ICR protozoan method for detecting Giardi cysts and Cryptosporidium oocysts in water by a fluorescent antibody procedure. Cincinnati, OH (26 Martin Luther King Dr., Cincinnati 45268): U.S. Environmental Protection Agency, OGWDW/TSD/WSTB, 1995.

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United States. Environmental Protection Agency. WSTB, ed. ICR protozoan method for detecting Giardi cysts and Cryptosporidium oocysts in water by a fluorescent antibody procedure. Cincinnati, OH (26 Martin Luther King Dr., Cincinnati 45268): U.S. Environmental Protection Agency, OGWDW/TSD/WSTB, 1995.

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Book chapters on the topic "Lambda fluorescent"

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Nyindodo-Ogari, Lilian, Steven D. Schwartzbach, Omar Skalli, and Carlos E. Estraño. "Localizing Proteins in Fixed Giardia lamblia and Live Cultured Mammalian Cells by Confocal Fluorescence Microscopy." In Methods in Molecular Biology, 93–111. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6352-2_6.

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"Induced Optical Natural Fluorescence Spectroscopy for Giardia lamblia Cysts." In Computational Optical Biomedical Spectroscopy and Imaging, 221–58. CRC Press, 2015. http://dx.doi.org/10.1201/b18024-13.

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Conference papers on the topic "Lambda fluorescent"

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Bargatin, I. V., Boris A. Grishanin, and Victor N. Zadkov. "Fluorescence and absorption properties of a driven lambda-system." In ICONO '98: Laser Spectroscopy and Optical Diagnostics--Novel Trends and Applications in Laser Chemistry, Biophysics, and Biomedicine, edited by Anatoli V. Andreev, Sergei N. Bagayev, Anatoliy S. Chirkin, and Vladimir I. Denisov. SPIE, 1999. http://dx.doi.org/10.1117/12.340122.

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Filippidis, George, Giannis Zacharakis, G. E. Kochiadakis, S. I. Chrysostomakis, P. E. Vardas, Costas Fotakis, and Theodore G. Papazoglou. "Spectroscopic fluorescence measurements of lamb and human heart tissue in vitro." In SPIE Proceedings, edited by Valery V. Tuchin. SPIE, 2003. http://dx.doi.org/10.1117/12.518767.

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Filippidis, G., G. Zacharakis, A. Katsamouris, S. Palsson, S. Montan, K. Svanberg, S. Andersson-Engels, et al. "In vitro and in vivo laser-induced fluorescence measurements of human and lamb heart tissue." In Biomedical Topical Meeting. Washington, D.C.: OSA, 1999. http://dx.doi.org/10.1364/bio.1999.btuc3.

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