Relevant bibliographies by topics / Biliverdin reductase

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Biliverdin reductase'

Author: Grafiati
Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "Biliverdin reductase"

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Valasinas, Aldonia, and Benjamin Frydman. "Reduction of Biliverdins to Bilirubins: Its Metabolic Regulation Under Various Physiological Conditions." Current Medicinal Chemistry 3, no. 4 (1996): 291–302. http://dx.doi.org/10.2174/092986730304220302113254.

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Abstract: Heme and hemoproteins are degraded in mammals by oxidation to biliverdins. These linear tetrapyrroles are reduced to bilirubins by a cytosolic biliverdin reductase (BvR) at the rate of 250-400 mg per day. While the bulk of biliary biliverdin is biliverdin IX α , other isomers such as biliverdins IXβ and IXγ are formed under conditions of oxidative stress by the chemical degradation of hemoproteins, or from the degradation of abnormal hemoglobins. Rat liver BvR was found to. be a NADPH-dependent reductase with a broad substrate specificity, which efficiently reduces a large number of
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SHALLOE, Fiona, Gordon ELLIOTT, Orla ENNIS та Timothy J. MANTLE. "Evidence that biliverdin-IXβ reductase and flavin reductase are identical". Biochemical Journal 316, № 2 (1996): 385–87. http://dx.doi.org/10.1042/bj3160385.

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A search of the database shows that human biliverdin-IXβ reductase and flavin reductase are identical. We have isolated flavin reductase from bovine erythrocytes and show that the activity co-elutes with biliverdin-IXβ reductase. Preparations of the enzyme that are electrophoretically homogeneous exhibit both flavin reductase and biliverdin-IXβ reductase activities; however, they are not capable of catalysing the reduction of biliverdin-IXα. Although there is little obvious sequence identity between biliverdin-IXα reductase (BVR-A) and biliverdin-IXβ reductase (BVR-B), they do show weak immuno
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Yoshinaga, T., Y. Sudo та S. Sano. "Enzymic conversion of α-oxyprotohaem IX into biliverdin IXα by haem oxygenase". Biochemical Journal 270, № 3 (1990): 659–64. http://dx.doi.org/10.1042/bj2700659.

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Conversion of four isomers of meso-oxyprotohaem IX into the corresponding biliverdin IX was attempted with a reconstituted haem oxygenase system in the presence of NADPH-cytochrome c reductase and NADPH. Only the alpha-isomer of meso-oxyprotohaem IX was converted effectively into biliverdin IX alpha, which was further reduced to bilirubin IX alpha by biliverdin reductase. Only trace amounts of biliverdins IX beta, IX gamma and IX delta were respectively formed from the incubation mixture of the corresponding oxyprotohaemin IX isomers with the complete haem oxygenase system under the same condi
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Kikuchi, A., S.-Y. Park, H. Miyatake, et al. "Structure of Biliverdin Reductase." Seibutsu Butsuri 40, supplement (2000): S122. http://dx.doi.org/10.2142/biophys.40.s122_3.

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CUNNINGHAM, Orla, Michael G. GORE та Timothy J. MANTLE. "Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXβ reductase (BVR-B)". Biochemical Journal 345, № 2 (2000): 393–99. http://dx.doi.org/10.1042/bj3450393.

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The initial-rate kinetics of the flavin reductase reaction catalysed by biliverdin-IXβ reductase at pH 7.5 are consistent with a rapid-equilibrium ordered mechanism, with the pyridine nucleotide binding first. NADPH binding to the free enzyme was characterized using stopped-flow fluorescence quenching, and a Kd of 15.8 μM was calculated. Equilibrium fluorescence quenching experiments indicated a Kd of 0.55 μM, suggesting that an enzyme-NADPH encounter complex (Kd 15.8 μM) isomerizes to a more stable ‘nucleotide-induced’ conformation. The enzyme was shown to catalyse the reduction of FMN, FAD a
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Rigney, E. M., O. Phillips, and T. J. Mantle. "Some physical and immunological properties of ox kidney biliverdin reductase." Biochemical Journal 255, no. 2 (1988): 431–35. http://dx.doi.org/10.1042/bj2550431.

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The liver, kidney and spleen of the mouse and rat and the kidney and spleen of the ox express a monomeric form of biliverdin reductase (Mr 34,000), which in the case of the ox kidney enzyme exists in two forms (pI 5.4 and 5.2) that are probably charge isomers. The livers of the mouse and rats express, in addition, a protein (Mr 46,000) that cross-reacts with antibodies raised against the ox kidney enzyme and may be related to form 2 described by Frydman, Tomaro, Awruch & Frydman [(1983) Biochim. Biophys. Acta 759, 257-263]. Higher-Mr forms appear to exist in the guinea pig and hamster. The
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Briz, Oscar, Rocio I. R. Macias, Maria J. Perez, Maria A. Serrano, and Jose J. G. Marin. "Excretion of fetal biliverdin by the rat placenta-maternal liver tandem." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 290, no. 3 (2006): R749—R756. http://dx.doi.org/10.1152/ajpregu.00487.2005.

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Fetal liver immaturity is accompanied by active heme catabolism. Thus fetal biliary pigments must be excreted toward the mother by the placenta. To investigate biliverdin handling by the placenta-maternal liver tandem, biliverdin-IXα was administered to 21-day pregnant rats through the jugular vein or the umbilical artery of an in situ perfused placenta. Jugular administration resulted in the secretion into maternal bile of both bilirubin and biliverdin (3:1). However, when biliverdin was administered to the placenta, most of it was transformed into bilirubin before being transferred to the ma
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Smith, Liam J., Seamus Browne, Adrian J. Mulholland та Timothy J. Mantle. "Computational and experimental studies on the catalytic mechanism of biliverdin-IXβ reductase". Biochemical Journal 411, № 3 (2008): 475–84. http://dx.doi.org/10.1042/bj20071495.

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BVR-B (biliverdin-IXβ reductase) also known as FR (flavin reductase) is a promiscuous enzyme catalysing the pyridine-nucleotide-dependent reduction of a variety of flavins, biliverdins, PQQ (pyrroloquinoline quinone) and ferric ion. Mechanistically it is a good model for BVR-A (biliverdin-IXα reductase), a potential pharmacological target for neonatal jaundice and also a potential target for adjunct therapy to maintain protective levels of biliverdin-IXα during organ transplantation. In a commentary on the structure of BVR-B it was noted that one outstanding issue remained: whether the mechani
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Schluchter, Wendy M., and Alexander N. Glazer. "Characterization of Cyanobacterial Biliverdin Reductase." Journal of Biological Chemistry 272, no. 21 (1997): 13562–69. http://dx.doi.org/10.1074/jbc.272.21.13562.

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O’Brien, Luke, Peter A. Hosick, Kezia John, David E. Stec, and Terry D. Hinds. "Biliverdin reductase isozymes in metabolism." Trends in Endocrinology & Metabolism 26, no. 4 (2015): 212–20. http://dx.doi.org/10.1016/j.tem.2015.02.001.

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Dissertations / Theses on the topic "Biliverdin reductase"

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Bisht, Kavita. "Anti-Inflammatory and Cell Signalling Effects of Biliverdin and Biliverdin Reductase." Thesis, Griffith University, 2014. http://hdl.handle.net/10072/368136.

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Despite advances in medical care and research, sepsis still poses a great threat to the health of society and remains a major cause of mortality and morbidity throughout the world. The progression of sepsis is driven by inflammatory processes. Stimuli, including endotoxin, play a crucial role in the initiation of inflammation via their interaction with molecules associated with the immune system. Among them, toll like receptors, complement receptor 5 a (C5aR) and cytokines are key factors in both promoting and aggravating inflammation. Therefore, compounds that can inhibit the activation of th
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Zhang, Zhaoshu. "INCREASE OF BASAL OXIDATIVE STRESS LEVELS AND IMPAIRMENT OF HEME OXYGENASE-1/BILIVERDIN REDUCTASE POST-TRANSLATIONAL MODIFICATION BY THE DEFECT OF PARKINSON-RELATED GENE OF PINK1." UKnowledge, 2014. http://uknowledge.uky.edu/chemistry_etds/40.

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Parkinson disease (PD) is the most common movement disorder and the second most common neurodegenerative disease. PINK1, PTEN-induced kinase 1, functions as a serine/threonine kinase as well as a protector of mitochondrial function. Mutations in PINK1 gene result in either mitochondria dysfunction or disruption of kinase signaling pathways involved in the pathogenesis of PD. In this thesis, oxidative stress levels were examined in the brain of PINK1 knockout mice, and also how heme oxygenase-1 and biliverdin reductase are affected in brain of PINK1 knockout mice. In addition, posttranslational
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Kubíčková, Kristýna. "Úloha oxidačního stresu v jaterní kancerogenezi." Doctoral thesis, 2020. http://www.nusl.cz/ntk/nusl-436707.

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This thesis focuses on the importance of heme catabolic pathway in hepatic carcinogenesis. Hepatocellular carcinoma (HCC) is the most common primary malignant liver tumour. It is primarily caused by hepatic cirrhosis or chronic viral hepatitis. Hepatic carcinogenesis is associated with increased oxidative stress. Thus, our study aimed to assess the expression of the genes involved in the homeostasis of oxidative stress in patients with HCC. The study was performed on patients with primary HCC (n = 29) and control subjects (n = 11), gene expressions of heme oxygenase 1 (HMOX1), biliverdin reduc
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Subhanová, Iva. "Katabolická dráha hemu u chronické hepatitidy C." Doctoral thesis, 2013. http://www.nusl.cz/ntk/nusl-327399.

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This thesis focuses on the importance of the heme catabolic pathway in chronic hepatitis C (HCV). The aim is mainly to investigate, whether expresion/activity of key enzymes of the heme catabolic pathway, heme oxygenase (HMOX) and biliverdin reductase (BLVRA) in the liver and blood (study A) or promoter variations of HMOX1 and UDP- glucuronosyltransferase (UGT1A1) (study B) may be associated with the progression of fibrosis and may also predict antiviral treatment outcome in patients chronically infected with HCV. We set up a new sensitive method to quantify HMOX activity by reduction gas chro
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Book chapters on the topic "Biliverdin reductase"

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Schomburg, Dietmar, Margit Salzmann, and Dörte Stephan. "Biliverdin reductase." In Enzyme Handbook. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-58051-2_97.

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Kamp, Marc Willem. "Biliverdin IX-Beta Reductase: Computational Studies." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_252.

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"Biliverdin Reductase." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_100098.

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Thompson, Richard. "Jaundice." In Oxford Textbook of Medicine. Oxford University Press, 2010. http://dx.doi.org/10.1093/med/9780199204854.003.1520_update_002.

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All haem molecules are degraded in macrophages by haem oxygenase to biliverdin, and thence by biliverdin reductase to bilirubin, which is selectively removed by hepatocytes from sinusoidal blood and then conjugated, mainly by one of the two specific isoforms of the microsomal enzyme UDP-glucuronyl (glucuronate-glucuronosyl) transferase, chiefly with two glucuronic acid moieties. Conjugated bilirubin is excreted into the bile by the anionic conjugate transporter protein (MRP2), but in many liver diseases it refluxes back into blood and—since it is water soluble and less firmly bound to albumin than unconjugated bilirubin—about 1% is filtered across the glomerular membrane and darkens the urine (choluria). In the distal intestine conjugated bilirubin is deconjugated and reduced to a series of uro- and stercobilinogens that give the normal colour to faeces. Some colourless urobilinogen is normally absorbed from the colon and undergoes an enterohepatic circulation, with a small amount being excreted in urine. If this biliary excretion is impaired in liver disease, or increased in haemolysis, then excess urobilinogen is excreted in urine, where it is easily detected by routine clinical ‘stix’....
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Maines, Mahin D., and Peter E. M. Gibbs. "Biliverdin Reductase: Its Multiple Functions in Cell Signaling and Role in Cytoprotection." In Handbook of Porphyrin Science. World Scientific Publishing Company, 2013. http://dx.doi.org/10.1142/9789814407755_0008.

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R., James. "Elucidating the Role of Biliverdin Reductase in the Expression of Heme Oxygenase-1 as a Cytoprotective Response to Stress." In Pharmacology. InTech, 2012. http://dx.doi.org/10.5772/33875.

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