Academic literature on the topic 'Zinc protoporphyrin IX'

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Journal articles on the topic "Zinc protoporphyrin IX"

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Nelson, Joanna C., Marie Westwood, K. R. Allen, K. E. Newton, and J. H. Barth. "The Ratio of Erythrocyte Zinc-Protoporphyrin to Protoporphyrin IX in Disease and its Significance in the Mechanism of Lead Toxicity on Haem Synthesis." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 35, no. 3 (1998): 422–26. http://dx.doi.org/10.1177/000456329803500313.

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Protoporphyrin and zinc-protoporphyrin were measured in the erythrocytes of normal subjects, workers exposed to lead and patients with iron deficiency and erythropoietic protoporphyria (EPP). Results showed significantly higher levels of zinc-protoporphyrin in the lead-exposed workers ( P < 0·0001), patients with iron deficiency ( P < 0·0001) and EPP patients ( P < 0·001) compared with normal subjects. The lead-exposed workers showed the highest levels of zinc-protoporphyrin, which were significantly greater than both the iron-deficient and EPP patients ( P < 0·0001). They also sho
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Wakamatsu, Jun-ichi, Nobutaka Hayashi, Takanori Nishimura, and Akihito Hattori. "Nitric oxide inhibits the formation of zinc protoporphyrin IX and protoporphyrin IX." Meat Science 84, no. 1 (2010): 125–28. http://dx.doi.org/10.1016/j.meatsci.2009.08.036.

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WAKAMATSU, Jun-ichi, Ayana KATO, Misako EZOE, and Takanori NISHIMURA. "Effect of zinc protoporphyrin IX on dietary zinc bioavailability." Nihon Chikusan Gakkaiho 86, no. 4 (2015): 481–89. http://dx.doi.org/10.2508/chikusan.86.481.

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ISHIKAWA, Hiroya, Taiki KAWABUCHI, Yuriko KAWAKAMI, Masahiko SATO, Masahiro NUMATA, and Kiyoshi MATSUMOTO. "Formation of Zinc Protoporphyrin IX and Protoporphyrin IX from Oxymyoglobin in Porcine Heart Mitochondria." Food Science and Technology Research 13, no. 1 (2007): 85–88. http://dx.doi.org/10.3136/fstr.13.85.

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Orfanos, Adam P., Robert Guthrie, David C. Jinks, and Daniel W. Vollmer. "Simultaneous assay of zinc protoporphyrin and protoporphyrin IX in dried blood." Clinica Chimica Acta 181, no. 2 (1989): 213–17. http://dx.doi.org/10.1016/0009-8981(89)90191-5.

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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 (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
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Benedini, Riccardo, Valeria Raja, and Giovanni Parolari. "Zinc-protoporphyrin IX promoting activity in pork muscle." LWT - Food Science and Technology 41, no. 7 (2008): 1160–66. http://dx.doi.org/10.1016/j.lwt.2007.08.005.

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Hirano, Chisato, and Toyoko Imae. "Electrochemical properties of protoporphyrin IX zinc(II) films." Journal of Colloid and Interface Science 280, no. 2 (2004): 478–83. http://dx.doi.org/10.1016/j.jcis.2004.08.027.

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De Maere, Hannelore, Marlena Jaros, Marta Dziewięcka, et al. "DETERMINATION OF HEMIN, PROTOPORPHYRIN IX, AND ZINC(II) PROTOPORPHYRIN IX IN PARMA HAM USING THIN LAYER CHROMATOGRAPHY." Journal of Liquid Chromatography & Related Technologies 37, no. 20 (2014): 2971–79. http://dx.doi.org/10.1080/10739149.2014.906995.

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Hennig, Georg, Christian Gruber, Michael Vogeser, et al. "Dual-wavelength excitation for fluorescence-based quantification of zinc protoporphyrin IX and protoporphyrin IX in whole blood." Journal of Biophotonics 7, no. 7 (2013): 514–24. http://dx.doi.org/10.1002/jbio.201200228.

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Dissertations / Theses on the topic "Zinc protoporphyrin IX"

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Tangar, Antonija. "Structure-Function Relationships in Hexacoordinate Heme Proteins: Mechanism of Cytoglobin Interactions with Exogenous Ligands." FIU Digital Commons, 2018. https://digitalcommons.fiu.edu/etd/3729.

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Cytoglobin (Cygb) and neuroglobin (Ngb) are among the newest members of vertebrate globin family characterized by a classical 3-over-3 α-helical fold and a heme prosthetic group capable of reversibly binding small ligands such as O2, CO and NO. The physiological functions of Cygb and Ngb remain to be determined; however, current data suggest that both proteins have a significant role in cytoprotection in hypoxic and genotoxic conditions. Cytoglobin and Ngb are distinct from their better-known counterparts, hemoglobin (Hb) and myoglobin (Mb), in several structural features. First, in the absenc
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Paganelli, Marcella Oliva. "Expressão, purificação e estudos da ferroquelatase de Bacillus subtilis." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/75/75133/tde-05102015-093500/.

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A cor vermelha brilhante característica do presunto Parma é resultante, principalmente, do pigmento Zinco-protoporfirina IX (ZnPP). A ZnPP é formada a partir da mioglobina por uma reação de transmetalação, catalisada pela enzima ferroquelatase (FECH), em que o íon de Fe(II) coordenado ao grupo heme é substituído pelo íon Zn(II). O presunto Parma apresenta uma maior estabilidade oxidativa em relação aos demais produtos cárneos curados além de não conter nitrito e nitrato, portanto, são considerados mais saudáveis. A utilização da FECH no processamento de carnes curadas pode permitir a produção
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Glaser, Patricia Anna [Verfasser], Patrick [Akademischer Betreuer] Meybohm, Patrick [Gutachter] Meybohm, and Erhard [Gutachter] Seifried. "Diagnostik einer eisendefizitären Erythropoese mittels nicht-invasiver Messung von Zink-Protoporphyrin-IX bei chirurgischen Patienten / Patricia Anna Glaser ; Gutachter: Patrick Meybohm, Erhard Seifried ; Betreuer: Patrick Meybohm." Frankfurt am Main : Universitätsbibliothek Johann Christian Senckenberg, 2021. http://d-nb.info/1236723287/34.

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Sumpena, Kadek Yulia Kesuma Wardhani, and 卡蒂克. "A Study on the Gas Sensing Properties of Protoporphyrin Zinc IX towards Amines." Thesis, 2007. http://ndltd.ncl.edu.tw/handle/sq9cna.

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碩士<br>國立臺灣科技大學<br>化學工程系<br>95<br>In this study, protoporphyrin zinc IX (ZnPP) is spun onto cleaned glass substrate. The changes of their UV-Visible spectra are investigated upon exposure to amine vapors. ZnPP as sensing materials shows good sensitivity, fast response and reproducible towards amine vapors sensing. In the presence of amine vapor, Soret band wavelength spectrum response of ZnPP will be red shifted. This red-shift phenomenon in the wavelength spectrum cause by changes in electronic structure of ZnPP. The experimental results are verified by TDDFT Calculation by Gaussian 03. Gaussi
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陳鈺菁. "Spectroscopy and Relaxation Dynamics of Protoporphyrin(IX) Zinc(II) in Solutions, inside AAO Nanotubes and in Combination with Apomyoglobin." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/84794992175849924489.

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碩士<br>國立交通大學<br>應用化學系所<br>93<br>The aggregation behaviors of Protoporphyrin (IX) Zinc (II) (ZnPP) in solutions, inside anodized aluminum oxide (AAO) nanoporous environments, and in combination with apomyoglobin (Apo-Mb) have been observed by using time-correlated single photon counting (TCSPC) technique. In ZnPP / THF solution, we observed a new band in addition to the Q (0,0) and Q (0,1) bands in the emission spectrum, and the fluorescence decays can be well described by a bi-exponential decay function with time coefficients of ~0.4 ns and ~2 ns. By observation of the change of the transients
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Book chapters on the topic "Zinc protoporphyrin IX"

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Shinoda, Yuichi, Makoto Suematsu, Yoshiyuki Wakabayashi, and Yuzuru Ishimura. "Effects of Zinc Protoporphyrin IX, a Heme Oxygenase Inhibitor, on Mitochondrial Membrane Potential in Rat Cultured Hepatocytes." In Oxygen Homeostasis and Its Dynamics. Springer Japan, 1998. http://dx.doi.org/10.1007/978-4-431-68476-3_75.

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Walke, Anna, Eric Suero Molina, Walter Stummer, and Simone König. "Protoporphyrin IX Analysis from Blood and Serum in the Context of Neurosurgery of Glioblastoma." In Mass Spectrometry [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.95042.

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Protoporphyrin IX (PPIX) is formed from δ-aminolevulinic acid (ALA) during heme biosynthesis. Due to its cyclic tetrapyrrole core structure, it absorbs in the visible region of the electromagnetic spectrum and is thus colored. Both ALA and PPIX have become of great interest to neurosurgery, because in high-grade glioma, ALA diffuses into the tumor and is converted to PPIX. Fluorescence-guided resection (FGR) takes advantage of both the enrichment of PPIX in the tumor and its fluorescent properties, which enable visualization of tumor tissue. ALA-mediated FGR thus maximizes the extent of resection with better prognosis for patients. Tumor cells are able to produce porphyrins naturally or after administration of ALA, which is also reflected in elevated plasma fluorescence of cancer patients. PPIX might thus serve as a biomarker for monitoring of the tumor burden. A liquid chromatography-mass spectrometry (LC-MS)-based method is presented to quantify PPIX in blood and serum in the context of current fluorescence-based diagnostics. The method is able to distinguish between zinc PPIX, a component of red blood cells of importance in the detection of lead poisoning and iron deficiency anemia, and metal-free PPIX. In a proof-of-principle study, it was used to follow a time course of a glioblastoma patient undergoing surgery and confirmed elevated PPIX blood levels before ALA administration. During surgery, these blood levels increased about four-fold. The here developed 10 min reversed-phase LC-target MS method now allows patient screening with high specificity and throughput.
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"Protoporphyrin-IX-Zink-Chelat." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_301404.

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Zhang, Zhijun, and Toyoko Imae. "Surface Enhanced Infrared Absorption and UV-Vis Spectroscopic Study of a Monolayer Film of Protoporphyrin IX Zinc (II) on Gold." In Studies in Surface Science and Catalysis. Elsevier, 2001. http://dx.doi.org/10.1016/s0167-2991(01)82159-5.

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Conference papers on the topic "Zinc protoporphyrin IX"

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Hennig, Georg, Michael Vogeser, Lesca M. Holdt, et al. "Dual-wavelength excitation to reduce background fluorescence for fluorescence spectroscopic quantitation of erythrocyte zinc protoporphyrin-IX and protoporphyrin-IX from whole blood and oral mucosa." In SPIE BiOS, edited by Gerard L. Coté. SPIE, 2014. http://dx.doi.org/10.1117/12.2039279.

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