1,3,6,7-Tetramethyl-4,5-dicarboxyethyl-2,8-divinylbilenone. Biosynthesized from hemoglobin as a precursor of bilirubin. Occurs in the bile of AMPHIBIANS and of birds, but not in normal human bile or serum.
A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.
Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.
Databases devoted to knowledge about specific genes and gene products.
A mixed function oxidase enzyme which during hemoglobin catabolism catalyzes the degradation of heme to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt. EC 1.14.99.3.
The complete genetic complement contained in the DNA of a set of CHROMOSOMES in a HUMAN. The length of the human genome is about 3 billion base pairs.
A ubiquitous stress-responsive enzyme that catalyzes the oxidative cleavage of HEME to yield IRON; CARBON MONOXIDE; and BILIVERDIN.
Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.
The terms, expressions, designations, or symbols used in a particular science, discipline, or specialized subject area.
The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)
Copies of a work or document distributed to the public by sale, rental, lease, or lending. (From ALA Glossary of Library and Information Science, 1983, p181)
A publication issued at stated, more or less regular, intervals.
"The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.
Critical and exhaustive investigation or experimentation, having for its aim the discovery of new facts and their correct interpretation, the revision of accepted conclusions, theories, or laws in the light of newly discovered facts, or the practical application of such new or revised conclusions, theories, or laws. (Webster, 3d ed)
Research that involves the application of the natural sciences, especially biology and physiology, to medicine.
A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.
Exclusive legal rights or privileges applied to inventions, plants, etc.
Compounds formed by the joining of smaller, usually repeating, units linked by covalent bonds. These compounds often form large macromolecules (e.g., BIOPOLYMERS; PLASTICS).
Treatment of diseases with biological materials or biological response modifiers, such as the use of GENES; CELLS; TISSUES; organs; SERUM; VACCINES; and humoral agents.
Complex pharmaceutical substances, preparations, or matter derived from organisms usually obtained by biological methods or assay.
Drugs that are used to treat RHEUMATOID ARTHRITIS.
Polymers of ETHYLENE OXIDE and water, and their ethers. They vary in consistency from liquid to solid depending on the molecular weight indicated by a number following the name. They are used as SURFACTANTS, dispersing agents, solvents, ointment and suppository bases, vehicles, and tablet excipients. Some specific groups are NONOXYNOLS, OCTOXYNOLS, and POLOXAMERS.
The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
The space between the arachnoid membrane and PIA MATER, filled with CEREBROSPINAL FLUID. It contains large blood vessels that supply the BRAIN and SPINAL CORD.
Bleeding into the intracranial or spinal SUBARACHNOID SPACE, most resulting from INTRACRANIAL ANEURYSM rupture. It can occur after traumatic injuries (SUBARACHNOID HEMORRHAGE, TRAUMATIC). Clinical features include HEADACHE; NAUSEA; VOMITING, nuchal rigidity, variable neurological deficits and reduced mental status.
One of three principal openings in the SUBARACHNOID SPACE. They are also known as cerebellomedullary cistern, and collectively as cisterns.
The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.
A plant genus of the family ARECACEAE. It is a tropical palm tree that yields a large, edible hard-shelled fruit from which oil and fiber are also obtained.
An order of fungi in the phylum BASIDIOMYCOTA having macroscopic basidiocarps. The members are characterized by their saprophytic activities as decomposers, particularly in the degradation of CELLULOSE and LIGNIN. A large number of species in the order have been used medicinally. (From Alexopoulos, Introductory Mycology, 4th ed, pp504-68)
Sequential operating programs and data which instruct the functioning of a digital computer.
A genus of basiodiomycetous fungi in the family Coriolaceae. Members are known for infesting wood.
A family of fungi, order POLYPORALES, found on decaying wood.
Auditory and visual instructional materials.
All of the divisions of the natural sciences dealing with the various aspects of the phenomena of life and vital processes. The concept includes anatomy and physiology, biochemistry and biophysics, and the biology of animals, plants, and microorganisms. It should be differentiated from BIOLOGY, one of its subdivisions, concerned specifically with the origin and life processes of living organisms.

Crystallization of recombinant human heme oxygenase-1. (1/201)

Heme oxygenase catalyzes the NADPH, O2, and cytochrome P450 reductase dependent oxidation of heme to biliverdin and carbon monoxide. One of two primary isozymes, HO-1, is anchored to the endoplasmic reticulum membrane via a stretch of hydrophobic residues at the C-terminus. While full-length human HO-1 consists of 288 residues, a truncated version with residues 1-265 has been expressed as a soluble active enzyme in Escherichia coli. The recombinant enzyme crystallized from ammonium sulfate solutions but the crystals were not of sufficient quality for diffraction studies. SDS gel analysis indicated that the protein had undergone proteolytic degradation. An increase in the use of protease inhibitors during purification eliminated proteolysis, but the intact protein did not crystallize. N-terminal sequencing and mass spectral analysis of dissolved crystals indicated that the protein had degraded to two major species consisting of residues 1-226 and 1-237. Expression of the 1-226 and 1-233 versions of human HO-1 provided active enzyme that crystallizes in a form suitable for diffraction studies. These crystals belong to space group P2(1), with unit cell dimensions a = 79.3 A, b = 56.3 A, c = 112.8 A, and beta = 101.5 degrees.  (+info)

Carbon monoxide stimulates the apical 70-pS K+ channel of the rat thick ascending limb. (2/201)

We have investigated the expression of heme oxygenase (HO) in the rat kidney and the effects of HO-dependent heme metabolites on the apical 70-pS K+ channel in the thick ascending limb (TAL). Reverse transcriptase-PCR (RT-PCR) and Western blot analyses indicate expression of the constitutive HO form, HO-2, in the rat cortex and outer medulla. Patch-clamping showed that application of 10 microM chromium mesoporphyrin (CrMP), an inhibitor of HO, reversibly reduced the activity of the apical 70-pS K+ channel, defined by NPo, to 26% of the control value. In contrast, addition of 10 microM magnesium protoporphyrin had no significant effect on channel activity. HO involvement in regulation of the apical 70-pS K+ channel of the TAL, was further indicated by the addition of 10 microM heme-L-lysinate, which significantly stimulated the channel activity in cell-attached patches by 98%. The stimulatory effect of heme on channel activity was also observed in inside-out patches in the presence of 0.5-1 mM reduced nicotinamide adenine dinucleotide phosphate. This was completely abolished by 10 microM CrMP, suggesting that a HO-dependent metabolite of heme mediated the effect. This was further supported by exposure of the cytosolic membrane of inside-out patches to a carbon monoxide-bubbled bath solution, which increased channel activity. Moreover, carbon monoxide completely abolished the effect of 10 microM CrMP on the channel activity. In contrast, 10 microM biliverdin, another HO-dependent metabolite of heme, had no effect. We conclude that carbon monoxide produced from heme via an HO-dependent metabolic pathway stimulates the apical 70-pS K+ channel in the rat TAL.  (+info)

The Arabidopsis thaliana HY1 locus, required for phytochrome-chromophore biosynthesis, encodes a protein related to heme oxygenases. (3/201)

The hy1 mutants of Arabidopsis thaliana fail to make the phytochrome-chromophore phytochromobilin and therefore are deficient in a wide range of phytochrome-mediated responses. Because this defect can be rescued by feeding seedlings biliverdin IXalpha, it is likely that the mutations affect an enzyme that converts heme to this phytochromobilin intermediate. By a combination of positional cloning and candidate-gene isolation, we have identified the HY1 gene and found it to be related to cyanobacterial, algal, and animal heme oxygenases. Three independent alleles of hy1 contain DNA lesions within the HY1 coding region, and a genomic sequence spanning the HY1 locus complements the hy1-1 mutation. HY1 is a member of a gene family and is expressed in a variety of A. thaliana tissues. Based on its homology, we propose that HY1 encodes a higher-plant heme oxygenase, designated AtHO1, responsible for catalyzing the reaction that opens the tetrapyrrole ring of heme to generate biliverdin IXalpha.  (+info)

Bacteriophytochromes: phytochrome-like photoreceptors from nonphotosynthetic eubacteria. (4/201)

Phytochromes are a family of photoreceptors used by green plants to entrain their development to the light environment. The distribution of these chromoproteins has been expanded beyond photoautotrophs with the discovery of phytochrome-like proteins in the nonphotosynthetic eubacteria Deinococcus radiodurans and Pseudomonas aeruginosa. Like plant phytochromes, the D. radiodurans receptor covalently binds linear tetrapyrroles autocatalytically to generate a photochromic holoprotein. However, the attachment site is distinct, using a histidine to potentially form a Schiff base linkage. Sequence homology and mutational analysis suggest that D. radiodurans bacteriophytochrome functions as a light-regulated histidine kinase, which helps protect the bacterium from visible light.  (+info)

Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXbeta reductase (BVR-B). (5/201)

The initial-rate kinetics of the flavin reductase reaction catalysed by biliverdin-IXbeta 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 K(d) of 15.8 microM was calculated. Equilibrium fluorescence quenching experiments indicated a K(d) of 0.55 microM, suggesting that an enzyme-NADPH encounter complex (K(d) 15.8 microM) isomerizes to a more stable 'nucleotide-induced' conformation. The enzyme was shown to catalyse the reduction of FMN, FAD and riboflavin, with K(m) values of 52 microM, 125 microM and 53 microM, respectively. Lumichrome was shown to be a competitive inhibitor against FMN, with a K(i) of 76 microM, indicating that interactions with the isoalloxazine ring are probably sufficient for binding. During initial experiments it was observed that both the flavin reductase and biliverdin reductase activities of the enzyme exhibit a sharp optimum at pH 5 in citrate buffer. An initial-rate study indicated that the enzyme obeys a steady-state ordered mechanism in this buffer. The initial-rate kinetics in sodium acetate at pH 5 are consistent with a rapid-equilibrium ordered mechanism, indicating that citrate may directly affect the enzyme's behaviour at pH 5. Mesobiliverdin XIIIalpha, a synthetic biliverdin which binds to flavin reductase but does not act as a substrate for the enzyme, exhibits competitive kinetics with FMN (K(i) 0.59 microM) and mixed-inhibition kinetics with NADPH. This is consistent with a single pyridine nucleotide site and competition by FMN and biliverdin for a second site. Interestingly, flavin reductase/biliverdin-IXbeta reductase has also been shown to exhibit ferric reductase activity, with an apparent K(m) of 2.5 microM for the ferric iron. The ferric reductase reaction requires NAD(P)H and FMN. This activity is intriguing, as haem cleavage in the foetus produces non-alpha isomers of biliverdin and ferric iron, both of which are substrates for flavin reductase/biliverdin-IXbeta reductase.  (+info)

Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1. (6/201)

Heme oxygenase converts heme to biliverdin, iron, and CO in a reaction with two established intermediates, alpha-meso-hydroxyheme and verdoheme. Transient kinetic studies show that the conversion of Fe(3+)-heme to Fe(3+)-verdoheme is biphasic. Electron transfer to the heme (0.11 s(-1) at 4 degrees C and 0.49 s(-1) at 25 degrees C) followed by rapid O(2) binding yields the ferrous dioxy complex. Transfer of an electron (0.056 s(-1) at 4 degrees C and 0.21 s(-1) at 25 degrees C) to this complex triggers the formation of alpha-meso-hydroxyheme and its subsequent O(2)-dependent fragmentation to Fe(3+)-verdoheme. The conversion of Fe(3+)-verdoheme to Fe(3+)-biliverdin is also biphasic. Thus, reduction of Fe(3+) to Fe(2+)-verdoheme (0.15 s(-1) at 4 degrees C and 0.55 s(-1) at 25 degrees C) followed by O(2) binding and an electron transfer produces Fe(3+)-biliverdin (0.025 s(-1) at 4 degrees C and 0.10 s(-1) at 25 degrees C). The conversion of Fe(3+)-biliverdin to free biliverdin is triphasic. Reduction of Fe(3+)-biliverdin (0.035 s(-1) at 4 degrees C and 0.15 s(-1) at 25 degrees C), followed by rapid release of Fe(2+) (0.19 s(-1) at 4 degrees C and 0.39 s(-1) at 25 degrees C), yields the biliverdin-enzyme complex from which biliverdin slowly dissociates (0.007 s(-1) at 4 degrees C and 0.03 s(-1) at 25 degrees C). The rate of Fe(2+) release agrees with the rate of Fe(3+)-biliverdin reduction. Fe(2+) release clearly precedes biliverdin dissociation. In the absence of biliverdin reductase, biliverdin release is the rate-limiting step, but in its presence biliverdin release is accelerated and the overall rate of heme degradation is limited by the conversion of Fe(2+)-verdoheme to the Fe(3+)-biliverdin.  (+info)

Influence of bilirubin and other antioxidants on nitrergic relaxation in the pig gastric fundus. (7/201)

1. The influence of several antioxidants (bilirubin, urate, ascorbate, alpha-tocopherol, glutathione (GSH), Cu/Zn superoxide dismutase (SOD) and the manganese SOD mimic EUK-8) on nitrergic relaxations induced by either exogenous nitric oxide (NO; 10(-5) M) or electrical field stimulation (4 Hz; 10 s and 3 min) was studied in the pig gastric fundus. 2. Ascorbate (5x10(-4) M), alpha-tocopherol (4x10(-4) M), SOD (300 - 1000 u ml(-1)) and EUK-8 (3x10(-4) M) did not influence the relaxations to exogenous NO. In the presence of GSH (5x10(-4) M), the short-lasting relaxation to NO became biphasic, potentiated and prolonged. Urate (4x10(-4) M) and bilirubin (2x10(-4) M) also potentiated the relaxant effect of NO. None of the antioxidants influenced the electrically evoked relaxations. 3. 6-Anilino-5,8-quinolinedione (LY83583; 10(-5) M) had no influence on nitrergic nerve stimulation but nearly abolished the relaxant response to exogenous NO. Urate and GSH completely prevented this inhibitory effect, while it was partially reversed by SOD and bilirubin. Ascorbate, alpha-tocopherol and EUK-8 were without effect. 4. Hydroquinone (10(-4) M) did not affect the electrically induced nitrergic relaxations, but markedly reduced NO-induced relaxations. The inhibition of exogenous NO by hydroquinone was completely prevented by urate and GSH. SOD and ascorbate afforded partial protection, while bilirubin, EUK-8 and alpha-tocopherol were ineffective. 5. Hydroxocobalamin (10(-4) M) inhibited relaxations to NO by 50%, but not the electrically induced responses. Full protection versus this inhibitory effect was obtained with urate, GSH and alpha-tocopherol. 6. These results strengthen the hypothesis that several endogenous antioxidant defense mechanisms, enzymatic as well as non-enzymatic, might play a role in the nitrergic neurotransmission process.  (+info)

Arabidopsis phytochromes C and E have different spectral characteristics from those of phytochromes A and B. (8/201)

The red/far-red light absorbing phytochromes play a major role as sensor proteins in photomorphogenesis of plants. In Arabidopsis the phytochromes belong to a small gene family of five members, phytochrome A (phyA) to E (phyE). Knowledge of the dynamic properties of the phytochrome molecules is the basis of phytochrome signal transduction research. Beside photoconversion and destruction, dark reversion is a molecular property of some phytochromes. A possible role of dark reversion is the termination of signal transduction. Since Arabidopsis is a model plant for biological and genetic research, we focussed on spectroscopic characterization of Arabidopsis phytochromes, expressed in yeast. For the first time, we were able to determine the relative absorption maxima and minima for a phytochrome C (phyC) as 661/725 nm and for a phyE as 670/724 nm. The spectral characteristics of phyC and E are strictly different from those of phyA and B. Furthermore, we show that both phyC and phyE apoprotein chromophore adducts undergo a strong dark reversion. Difference spectra, monitored with phycocyanobilin and phytochromobilin as the apoprotein's chromophore, and in vivo dark reversion of the Arabidopsis phytochrome apoprotein phycocyanobilin adducts are discussed with respect to their physiological function.  (+info)

Hemorrhagic shock and resuscitation induces pulmonary inflammation that leads to acute lung injury. Biliverdin, a metabolite of heme catabolism, has been shown to have potent cytoprotective, anti-inflammatory, and anti-oxidant effects. This study aimed to examine the effects of intravenous biliverdin administration on lung injury induced by hemorrhagic shock and resuscitation in rats. Biliverdin or vehicle was administered to the rats 1 h before sham or hemorrhagic shock-inducing surgery. The sham-operated rats underwent all surgical procedures except bleeding. To induce hemorrhagic shock, rats were bled to achieve a mean arterial pressure of 30 mmHg that was maintained for 60 min, followed by resuscitation with shed blood. Histopathological changes in the lungs were evaluated by histopathological scoring analysis. Inflammatory gene expression was determined by Northern blot analysis, and oxidative DNA damage was assessed by measuring 8-hydroxy-2 deoxyguanosine levels in the lungs. Hemorrhagic ...
Biliverdin reductase (BVR) is an enzyme (EC 1.3.1.24) found in all tissues under normal conditions, but especially in reticulo-macrophages of the liver and spleen. BVR facilitates the conversion of biliverdin to bilirubin via the reduction of a double-bond between the second and third pyrrole ring into a single-bond. There are two isozymes, in humans, each encoded by its own gene, biliverdin reductase A (BLVRA) and biliverdin reductase B (BLVRB). BVR acts on biliverdin by reducing its double-bond between the pyrrole rings into a single-bond. It accomplishes this using NADPH + H+ as an electron donor, forming bilirubin and NADP+ as products. BVR catalyzes this reaction through an overlapping binding site including Lys18, Lys22, Lys179, Arg183, and Arg185 as key residues. This binding site attaches to biliverdin, and causes its dissociation from heme oxygenase (HO) (which catalyzes reaction of ferric heme --> biliverdin), causing the subsequent reduction to bilirubin. BVR is composed of two ...
Catalyses the two-electron reduction of biliverdin IXalpha at the C15 methine bridge. It has been proposed that this enzyme and EC 1.3.7.3, phycoerythrobilin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXalpha into phycoerythrobilin ...
Monoklonale und polyklonale Biliverdin Reductase Antikörper für viele Methoden. Ausgesuchte Qualitäts-Hersteller für Biliverdin Reductase Antikörper. Hier bestellen.
The Effects of Exercise Training and High Triglyceride Diet in an Estrogen Depleted Rat Model: The Role of the Heme Oxygenase System and Inflammatory Processes in Cardiovascular Risk
Complete information for BLVRA gene (Protein Coding), Biliverdin Reductase A, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
During the work for this thesis cellular and molecular approaches were used to study photomorphogenesis in the mosses Ceratodon purpureus and Physcomitrella patens. Phycocyanobilin, which substitutes for the phytochrome chromophore phytochromobilin, was injected into protonema tip cells of aphototropic Ceratodon mutants. This led in ~70 % of the filaments to a clear phototropic response and elevated chlorophyll levels in red light. The studies implied the existence of an extreme stable subfraction of holophytochrome, localized apparently to the apex of the tip cell. Injections of expression plasmids carrying for heme oxygenase genes from rat, Arabidopsis and Ceratodon (CpHO1) indicate that the mutants lack the enzymic activity of this gene product. In ~40 % injected filaments the wildtype phenotype could be restored. A GFP-CpHO1 fusion protein expressed from an appropriate plasmid showed that the enzyme is localized to the plastids. However, both plastidic and cytosolic enzymes were able to ...
Phytochromes are modular photoreceptors of plants, bacteria and fungi that use light as a source of information to regulate fundamental physiological processes. Interconversion between the active and inactive states is accomplished by a photoinduced reaction sequence which couples the sensor with the output module. However, the underlying molecular mechanism is yet not fully understood due to the lack of structural data of functionally relevant intermediate states. Here we report the crystal structure of a Meta-F intermediate state of an Agp2 variant from Agrobacterium fabrum. This intermediate, the identity of which was verified by resonance Raman spectroscopy, was formed by irradiation of the parent Pfr state and displays significant reorientations of almost all amino acids surrounding the chromophore. Structural comparisons allow identifying structural motifs that might serve as conformational switch for initiating the functional secondary structure change that is linked to the (de-)activation of
Biliverdin definition, a dark-green bile pigment, C 33 H 34 O 6 N 4 , formed as a breakdown product of hemoglobin and converted in humans to bilirubin. See more.
The ability to accurately sense light governs everything from seed germination, photosynthesis and pigmentation to patterns of growth and flowering. Now, University of Wisconsin-Madison scientists have obtained a detailed map of one of biologys most important light detectors, a protein found in many species across lifes plant, fungal and bacterial kingdoms. Scientists can now find out the secrets of how plants, in particular, react to light, allowing for a host of manipulations that could have a big impact on agriculture.. According to the university, a team of scientists from UW-Madison report in the Nov. 17 issue of the journal Nature that they have obtained the crystal structure of a phytochrome from a bacterium, the first such light-gathering structure depicted for all of biology. The structure of the bacterial phytochrome, according to the report, suggests its architecture first arose a billion or so years ago in a common ancestor and is shared among not only bacteria but also plants and ...
TY - JOUR. T1 - The effects of exercise training and high triglyceride diet in an estrogen depleted rat model. T2 - The role of the heme oxygenase system and inflammatory processes in cardiovascular risk. AU - Varga, Csaba. AU - Veszelka, Médea. AU - Kupai, Krisztina. AU - Börzsei, Denise. AU - Deim, Zoltán. AU - Szabó, Renáta. AU - Török, Szilvia. AU - Priksz, Dániel. AU - Gesztelyi, Rudolf. AU - Juhász, Béla. AU - Radak, Zsolt. AU - Pósa, Anikó. PY - 2018/1/1. Y1 - 2018/1/1. N2 - Cardiovascular morbidity and mortality of premenopausal women are significantly lower compared to men of similar age. However, this protective effect evidently decreases after the onset of menopause. We hypothesized that physical exercise could be a potential therapeutic strategy to improve inflammatory processes and cardiovascular antioxidant homeostasis, which can be affected by the loss of estrogen and the adverse environmental factors, such as overnutrition. Ovariectomized (OVX, n= 40) and ...
Jaundice, marked by yellowing of the skin, is common in infants, but also a symptom of various adult diseases. This discoloration is caused by excess bilirubin (BR), the substance that gives bile its yellow tinge. However, BR is also a vital antioxidant, which at healthy levels protects cells against peroxide damage. Its production in the body, though, has long been a source of uncertainty.. Now, a Japanese research collaboration involving Osaka University believes it has the answer. BR is already known to be produced from a related chemical, biliverdin (BV), by the enzyme biliverdin reductase (BVR). The enzyme wraps around BV and transfers two hydrogen atoms - one positive and one negative - to produce the yellow antioxidant. However, biologists could not establish which part of the enzyme was chemically involved in the process (the active site), or where the positive hydrogen came from. The findings were recently reported in Nature Communications.. Previous studies used BVR from rats, and ...
BVR Hottest Shape produk keluaran terbaru daripada Belle Vous Resources (BVR).Losyen yang mewangi membelai sambil buang lemak-lemak yang berlipat-lipat di badan.Losyen perlangsingan yang diformula khusus menggunakan bahan terbaik dan terpilih untuk merawat dan memecahkan berinci-inci lemak degil tubuh anda.BVR Hottest Shape… Maklumat Lanjut →. ...
Ya Allah, Murahkan Rezeki Bagiku ..... Ya Allah, apabila rezekiku ada di langit, maka turunkanlah, apabila di dalam bumi maka keluarkanlah, apabila di laut maka naikkanlah, apabila jauh maka dekatkanlah, sekiranya dekat maka permudahkanlah, dan sekiranya sedikit maka perbanyakkanlah dan sekiranya sedia banyak maka permudahkanlah untuk mendapatkannya , juga berilah keberkatan terhadap rezeki tersebut dan berikanlah rezeki padaku sebagaimana yang kujangka, dengan rezeki yang halal dan baik, serta banyak lagi keberkatan sehinggakan kutidak memerlukan sesiapa selain dari-Mu, dan jadikanlah kedua tanganku ini berada di atas dengan suka memberi dan menderma, dan jangan jadikan dua tanganku ini di bawah dengan suka meminta-minta, sesungguhnya Engkau amat berkuasa ke atas setiap sesuatu . ...
Heme oxygenase or haem oxygenase (HO) is an enzyme that catalyzes the degradation of heme. This produces biliverdin, ferrous iron, and carbon monoxide. There is limited evidence that levels of heme oxygenase are positive predictors of metabolic disease, insulin resistance, and metaflammation. Heme oxygenase cleaves the heme ring at the alpha-methene bridge to form either biliverdin or, if the heme is still attached to a globin, verdoglobin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. The reaction comprises three steps, which may be: Heme b3+ + O 2 + NADPH + H+ → α-meso-hydroxyheme3+ + NADP+ + H 2O α-meso-hydroxyheme3+ + H+ + O 2 → verdoheme4+ + CO + H2O verdoheme4+ + 7/2 NADPH + O 2+ 3/2 H+ → biliverdin + Fe2+ + 7/2 NADP+ + H 2O The sum of these reactions is: Heme b3+ + 3O 2 + 9/2 NADPH + 7/2 H+ → biliverdin + Fe2+ + CO + 9/2 NADP+ + 3H 2O If the iron is initially in the +2 state, the reaction could be: Heme b2+ + 3O2 + 4 NADPH + 4 H+ → biliverdin + ...
Phytochromobilin (P Phi B), the chromophore of plant phytochromes, is difficult to isolate because phytochromes occur at very low concentrations in plants. It is, therefore, frequently replaced in plant phytochrome studies by phycocyanobilin, which is abundant in cyanobacteria. P Phi B is also an attractive chromophore for far-red emitting chromoproteins. In this work, we design and optimize a simple method to efficiently isolate useful quantities of P Phi B: The chromophore is generated in Escherichiacoli and transiently bound to a tailored chromophore-binding domain of ApcE2, the apo-protein of a core-membrane linker, from which it can subsequently be released. The ease and effectiveness of this method hinges not only on the enhanced biosynthesis of P Phi B in the presence of the ApcE2 construct from Synechococcus sp. PCC7335, but also on the noncovalent binding of the pigment to its apo-protein. The isolated P Phi B was successfully incorporated into phytochrome-related assemblies, and ...
1. In four animals with a bile duct-ureter anastomosis and without disturbance due to obstruction or absorption, the total quantity of bile pigment output during a day under normal conditions varied from 0.0618 to 0.0678 gm. These figures are practically identical with those of Stadelmann (9, 10) but lower than those given by Hooper and Whipple (7), who find that the average bile pigment excretion amounts to about 1 mg. per pound of body weight per 6 hours.. 2. In all the experiments there is definite evidence of a decrease in bile pigment elimination after splenectomy. This is true not only of the elimination when no hemolytic agent is administered but also when excessive blood destruction is caused. Under the latter circumstances the amount of bile pigment is greatly increased but never reaches the high level of blood destruction before splenectomy.. 3. These observations appear to show conclusively that the absence of the spleen influences the formation of bile pigment. To what extent the ...
To get an adequate understanding of the problem of jaundice in neonates, to know a little about the metabolism of bilirubin in neonates. Bilirubin is a product that is toxic and must be issued by the body. Most of the bilirubin is derived from blood hemoglobin degradation and partly from the hem free or eritropoesis ineffective. Bilirubin formation was initiated by the oxidation process that produces biliverdin and several other substances. Biliverdin is reduced and this is a free bilirubin or bilirubin IX alpha. This substance is difficult to dissolve in water but soluble in fat, therefore had the difficult nature of the lipophilic and easily excreted through biological membranes such as the placenta and blood brain barrier. Free bilirubin is then fused with albumin and transported to the liver. In the hepatic uptake mechanism occurs, so that bilirubin is bound by the receptor liver cell membrane and into the liver cell. As soon as there is in the heart cells, occur persnyawaan with ligandin ...
Dr. Anne Eglash answered: Several causes: Your ALT, AST, and bilirubin are liver tests. These can be elevated for many reasons...
pep:known chromosome:VEGA66:2:180597790:180622189:1 gene:OTTMUSG00000016344 transcript:OTTMUST00000039291 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Col9a3 description:procollagen type IX alpha 3 ...
The majority of bilirubin (80%) is produced from the degradation of hemoglobin from erythrocytes undergoing normal (removal of aged or effete cells) or abnormal destruction (i.e. intravascular or extravascular hemolysis) within mononuclear phagocytes (principally splenic, hepatic and bone marrow macrophages). A small percentage (20%) is derived from the catabolism of various hepatic hemoproteins (myoglobin, cytochrome P450) as well as from the overproduction of heme from ineffective erythropoiesis in the bone marrow.. Within macrophages, a free heme group (iron + porphyrin ring) is oxidized by microsomal heme oxygenase into biliverdin and the iron is released (the iron is then stored as ferritin or released into plasma, where it is bound to the transport protein, transferrin). Biliverdin reductase then reduces the green water-soluble biliverdin into unconjugated (water-insoluble but lipid soluble) bilirubin. Heme oxygenase is also located in renal and hepatic parenchyma, enabling these tissues ...
The biochemistry of the porphyrins and of the bile pigments are closely related topics. Heme is synthesized from porphyrins and iron, and the products of degradation of heme are the bile pigments and iron. The biochemistry of the porphyrins and of heme is basic to understanding the varied functions of hemoproteins, and the porphyrias, a group of diseases caused by abnormalities in the pathway of porphyrin biosynthesis. A much more common clinical condition is jaundice, a consequence of an elevated level of plasma bilirubin, due either to overproduction of bilirubin or to failure of its excretion. Jaundice occurs in numerous diseases ranging from hemolytic anemias to viral hepatitis and to cancer of the pancreas. ...
Materials. [2-14C]-glycine (57 mCi/mmol) was purchased from ICN Biomedicals (Cleveland, OH), and δ-[3,5-3H]aminolevulinic acid (1.87 Ci/mmol) was obtained from DuPont NEN Radiochemicals (Wilmington, DE). Zn protoporphyrin 9 (ZnPP9) was obtained from Porphyrin Products.. Assay of heme oxygenase activity. Microsomes were prepared from each tissue as previously described (Schacter, 1978). Heme oxygenase activity was measured by the method of Tenhunen et al. (1970a). Briefly, the 1.0 ml reaction mixture contained 0.1 m potassium phosphate buffer (pH 7.4), microsomes (1 mg of protein), 17 μm hemin, 180 μm NADPH, and purified biliverdin reductase (step 3, 1 mg of protein) (Tenhunen et al., 1970b). The reaction was performed for 10 min at 37°C. Blank assays were conducted in the absence of NADPH. The rate of bilirubin formation was calculated from the rate of increase in absorbance (468 nm). The extinction coefficient, obtained with standards in the reaction mixture, was 13.9 mm−1cm−1.. Cell ...
E photoisomerization of the tetrapyrrole chromophore, believed to occur at C15 of the methine bridge between rings C and D. Recent crystal structures show that ring D in Pr is less tightly packed by the protein than rings A, B and C, which should favor the C15 reaction over reactions at C4 (AB methine bridge) and C10 (BC). In the present work, quantum chemical methods are used to establish the intrinsic reactivity of the chromophore towards all three possible Z ...
A heme group is a prosthetic group consisting of a protoporphyrin ring and a central iron (Fe) atom. A protoporphyrin ring is made up of four pyrrole rings linked by methine bridges. Four methyl, two vinyl, and two propionate side chains are attached. Heme of hemoglobin protein is a prosthetic group of heterocyclic ring of porphyrin of an iron atom; the biological function of the group is for delivering oxygen to body tissues, such that bonding of ligand of gas molecules to the iron atom of the protein group changes the structure of the protein by amino acid group of histidine residue around the heme molecule. The iron lies in the center is an organic component called protoporphyrin, which is bound to four pyrrole nitrogen atom linked by a methine bridge that forms a tetrapyrrole ring. The iron can either be in the ferrous (Fe2+) or the ferric (Fe3+) oxidation state. However, it is only able to bind to oxygen when in the ferrous state. The iron can form two additional bonds in fifth and in sixth ...
Bile - What causes green bile? Chemical properties. Biliverdin is a green tetrapyrrolic bile pigment, and is a product of heme/redcell breadown. Biliverdin is further broken down to bilirubin for easier excretion to the outside world (also into urobilinogen in urine-as mild yellow). This compound absorbs green light, thus appears green to your eyes! (put in dard room=brown/black). I think u maybe asking why u threw up green? Consult doc. Good luck.
Hem (rdeči pigment), se z encimom hemoksigenazo spremeni v zeleni biliverdin, ki se naprej reducira z biliverdin reduktazo v rumenkasto-oranžni bilirubin. Nastali pigment ni topen v vodi, zato se po krvi prenaša vezan na albumin. Ko prispe do jeter, se presnovi v vodotopno in nestrupeno obliko. Ta proces pretvorbe imenujemo konjugacija, pri kateri poteka esterifikacija z glukuronsko kislino. Po konjugaciji se izloča z žolčem v prebavni kanal. V prebavilih ga bakterije spremenijo v brezbarvni urobilinogen. Ta se v debelem črevesju pretvori v sterkobilinogen in naprej v sterkobilin, ki daje značilno barvo blatu. Urobilinogen se delno reabsorbira v kri (enterohepatični obtok) in vstopi nazaj v jetra ter ponovno izloči z žolčem. Nekaj malega pa se ga izloči z urinom kot rumeni urobilin. ...
New hope in the fight against cardiovascular disease has arrived, following breakthrough research identifying a pigment in our bile which could protect us.
A liquid crystal host-guest system composed of achiral organic molecules (host) and colored chiral metal complexes (guest) was fabricated to sense both right- and left-handed circularly polarized light (r- and l-CPL), depending on the guest (dopant) concentration. The CPL-sensing can be reversibly turned on and off
Heme oxygenase (HO) is a microsomal enzyme involved in cellular response to oxidative stress. HO oxidatively cleaves the heme ring at the alpha…
Old red blood cells are broken down in the liver, spleen and bone marrow. Some of the iron from the Hb is stored, and used for making new Hb, some of it is turned into bile pigment and excreted ...
Vmn2r51 - mouse gene knockout kit via CRISPR, 1 kit. |dl||dt|Kit Component:|/dt||dd|- |strong|KN319181G1|/strong|, Vmn2r51 gRNA vector 1 in |a href=http://www.origene.com/CRISPR-CAS9/Detail.
Using recently developed molecular-shape description algorithms, we searched the Available Chemical Directory for known compounds similar in shape to the potent HIV-1 protease inhibitor Merck L-700,417; 15 compounds most similar in shape to the inhibitor were selected for testing in vitro. Four of these inhibited the protease at 100 µM or less and the most active of the four were the naturally occurring pigments biliverdin and bilirubin. Biliverdin and bilirubin inhibited recombinant HIV-1 protease in vitro at pH 7.8 with Ki values of approx. 1 µM, and also inhibited HIV-2 and simian immunodeficiency virus proteases. The related pyrrolic pigments stercobilin, urobilin, biliverdin dimethyl ester and xanthobilirubic acid showed similar inhibitory activity at low micromolar concentrations. Biliverdin, bilirubin and xanthobilirubic acid did not inhibit viral polyprotein processing in cultured cells, but they reduced viral infectivity significantly. At 100 µM, xanthobilirubic acid affected viral ...
TY - JOUR. T1 - Bilirubin, renal hemodynamics, and blood pressure. AU - Stec, David E.. AU - Hosick, Peter A.. AU - Granger, Joey P.. PY - 2012/9/13. Y1 - 2012/9/13. N2 - Bilirubin is generated from the breakdown of heme by heme oxygenase and the reduction of biliverdin by the enzyme biliverdin reductase. Several large population studies have reported a significant inverse correlation between plasma bilirubin levels and the incidence of cardiovascular disease. Protection from cardiovascular disease is also observed in patients with Gilberts syndrome which is a disease characterized by mutations in hepatic UGT1A1, the enzyme responsible for the conjugation of bilirubin into the bile. Despite the strong correlation between plasma bilirubin levels and the protection from cardiovascular disease, the mechanism by which increases in plasma bilirubin acts to protect against cardiovascular disease is unknown. Since the chronic antihypertensive actions of bilirubin are likely due to its renal actions, ...
TY - JOUR. T1 - Reaction intermediates in the heme degradation reaction by HutZ from. T2 - Vibrio cholerae. AU - Uchida, Takeshi. AU - Sekine, Yukari. AU - Dojun, Nobuhiko. AU - Lewis-Ballester, Ariel. AU - Ishigami, Izumi. AU - Matsui, Toshitaka. AU - Yeh, Syun Ru. AU - Ishimori, Koichiro. PY - 2017/1/1. Y1 - 2017/1/1. N2 - HutZ is a heme-degrading enzyme in Vibrio cholerae. It converts heme to biliverdin via verdoheme, suggesting that it follows the same reaction mechanism as that of mammalian heme oxygenase. However, none of the key intermediates have been identified. In this study, we applied steady-state and time-resolved UV-vis absorption and resonance Raman spectroscopy to study the reaction of the heme-HutZ complex with H2O2 or ascorbic acid. We characterized three intermediates: oxyferrous heme, meso-hydroxyheme, and verdoheme complexes. Our data support the view that HutZ degrades heme in a manner similar to mammalian heme oxygenase, despite their low sequence and structural ...
Title:Application of Carbon Monoxide for Transplantation. VOLUME: 13 ISSUE: 6. Author(s):Atsunori Nakao and Yoshiya Toyoda. Affiliation:E1551, Biomedical Science Tower, 200 Lothrop Street, Pittsburgh, PA, 15213, USA.. Keywords:Carbon monoxide, transplantation, ischemia reperfusion, rejection. Abstract:Carbon monoxide (CO) is an invisible, chemically inert, colorless and odorless gas and is toxic at high concentrations due to its interference with oxygen delivery. However, CO is endogenously and physiologically generated in mammalian cells via the catabolism of heme in a rate-limiting step of heme oxygenase systems, and CO potently protects against cellular injury. CO relaxes blood vessels and exerts anti-thrombotic effects by inhibiting platelet aggregation and derepressing fibrinolysis. In addition, CO reduces ischemia/reperfusion injury and inflammatory responses. CO inhibits apoptosis of endothelial and epithelial cells and reduces proliferation of smooth muscle cells, fibroblasts and T ...
Background and aims: Bilirubin is an orange-yellow tetrapyrrole produced from the breakdown of heme by mammals and some other vertebrates. Plants, algae, and cyanobacteria synthesize molecules similar to bilirubin, including the protein-bound bilins and phytochromobilin which harvest or sense light. Recently, we discovered bilirubin in the arils of Strelitzia nicolai, the White Bird of Paradise Tree, which was the first example of this molecule in a higher plant. Subsequently, we identified bilirubin in both the arils and flowers of Strelitzia reginae, the Bird of Paradise Flower. In the arils of both species, bilirubin is present as the primary pigment, and thus functions to produce color. Previously, no tetrapyrroles were known to generate display color in plants. We were therefore interested in determining whether bilirubin is broadly distributed in the plant kingdom, and whether it contributes to color in other species.
Phytochromes are a widespread family of red/far-red responsive photoreceptors first discovered in plants, where they constitute one of the three main classes of photomorphogenesis regulators. All phytochromes utilize covalently attached bilin chromophores that enable photoconversion between red-abso …
Vanadate oxidation The bilirubin is oxidized by vanadate at about pH 3 to produce biliverdin. In the presence of the detergent and the vanadate, both conjugated (direct) and unconjugated bilirubin are oxidized. This oxidation reaction causes the decrease in the optical density of the yellow color, which is specific to bilirubin. The decrease in optical density at 451 nm is proportional to the total bilirubin concentration in the sample.(Metoden tatt i bruk: 5/1-06 ...
Buy our Recombinant Human Heme Oxygenase 1 protein. Ab86919 is a protein fragment produced in Escherichia coli and has been validated in SDS-PAGE. Abcam…
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2016 - 2019. [37] Byeongjun Yu, Dobeen Hwang, Hyungsu Jeon, Hyungjun Kim, Yonghyun Lee, Hyeongseop Keum, Jinjoo Kim, Dong Yun Lee, Yujin Kim, Junho Chung, Sangyong Jon. A hybrid platform based on a bispecific peptide-antibody complex for targeted cancer therapy Angewantde chemie. 2019 Feb 11:58(7):2005-2019 (IF 12.257). [36] Hyungjun Kim, Dobeen Hwang, Minsuk Choi, Soyoung Lee, Sukmo Kang, Yonghyun Lee, Sunghyun Kim, Junho Chung, and Sangyong Jon. Antibody-assisted delivery of a peptide-drug conjugate for targeted cancer therapy Molecular Pharmaceutics. 2018 Dec 6:16(1):165-172 (IF 4.396). [35] Joon Nam*, Yonghyun Lee*, Yejin Yang, Seongkeun Jung, Wooseong Kim, Jin-Wook Yoo, Jeon-Ok Moon, Changyong Lee, Hae Young Chung, Minsoo Kim, Sangyong Jon, and Yunjin Jung. Is it worth expending energy to convert biliverdin into bilirubin? Free Radical Biology and Medicine. 2018 Aug 20;124:232-240. (IF 5.657). *These authors contributed equally to this work.. [34] Soyoung Lee, Yonghyun Lee, Hyungjun ...
As Greenery is the nominated colour of the year, Im motivated to use this colour in a meaningful way (also, in part as a visual time stamp) in my next biomedical animation. However, I am struggling to associate the colour with new beginnings. In medicine, bile is green and green is also the colour of a mature bruise. In this case it is biliverdin, which is the breakdown product of haemoglobin that causes the green tinge.. In biomedical animation, it is fresh pinks and soft reds that elicit a feeling of health and vitality, whereas green is typically a symbol of sickness, used to describe decay, bacteria and infection.. ...
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Name:C.I.Basic Red 12,C.I.48070 Molecular Structure: Methine class C.I.Basic Red 12,C.I.48070,CAS 6320-14-5,392.96,C25H29ClN2,Basic Red FF,Basic Red AFF,Basic Red FP,Basic Red FF,Basic Red PL-F C.I.Basic Red 12,C.I.48070,CAS 6320-14-5,392.96,C25H29ClN2,Basic Red FF Molecular Formula:C25H29ClN2 Molecular Weight: 392.96 CAS Registry Number:6320-14-5
Anoxygenic phototrophic bacteria have the ability to transform light energy into biochemical amenable energy for their growth and motion. The collection of light and its transformation into chemical energy are mediated by the so-called photosynthetic apparatus. This complex system is composed of three multimeric transmembrane protein complexes: the light-harvesting (LH) complexes, the photochemical reaction center (RC), and the cytochrome bc 1 complex located in the intracytoplasmic membrane. Light collected by the peripheral LH complexes is transferred first to the LH1 complex, which absorbs at around 870 nm, and then to the RC, where a charge separation occurs. This initiates a cyclic electron transfer between the RC and cytochrome bc 1 via electron carrier proteins in the periplasmic space and quinone molecules in the membrane. This cyclic electron transfer is coupled to the translocation of protons and to the formation of a proton motive force across the inner membrane, ultimately used for ...
Heme oxygenase-1 (HO-1) is a microsomal enzyme that degrades heme, a prosthetic group of the heme protein family (e.g., hemoglobin), into the bile pigment biliverdin. Biliverdin is subsequently converted to bilirubin, carbon monoxide, and reduced iron. Bilirubin has an anti-inflammatory effect and is part of the oxidative stress response due to its strong free radical scavenging activity, whereas carbon monoxide has a vasodilatory effect on organ blood flow ...
Heme oxygenase-1 (HO-1) is a microsomal enzyme that degrades heme, a prosthetic group of the heme protein family (e.g., hemoglobin), into the bile pigment biliverdin. Biliverdin is subsequently converted to bilirubin, carbon monoxide, and reduced iron. Bilirubin has an anti-inflammatory effect and is part of the oxidative stress response due to its strong free radical scavenging activity, whereas carbon monoxide has a vasodilatory effect on organ blood flow ...
Despite the absence of known eggshell pigments (biliverdin and protoporphyrin), we found differences in the UV-reflectance of the four species eggshells. We showed that removal of the outer layers of avian eggshells that contain a cuticle increases UV-chroma, suggesting that the cuticle modulates UV-reflectance of white eggshells. This is likely achieved by selective absorption of UV-wavelengths by the compounds in the cuticle. The effects of the cuticle on eggshell coloration are particularly important, because the composition, thickness and extent of coverage of the cuticle (and thus potentially colour of the shell) can vary according to female age and egg freshness (Rodríguez-Navarro et al., 2013). These results highlight the importance of factors other than biliverdin and protoporphyrin in influencing avian eggshell coloration.. Eggshell colour varied across these unpigmented eggshells, and differed from that of pure calcite, even after their cuticles were removed (supplementary material ...
Cairan empedu berasal dari penghancuran hemoglobin dari eritrosit yang telah tua. Hemoglobin ini akan di uraikan menjadi hemin, zat besi, dan globin. Zat besi dan globin akan di simpan di dalam hati kemudian di kirim ke sum-sum tulang merah. Zat-zat tersebut digunakan dalam pembentukan antibodi atau hemoglobin baru. Sementara itu, Hemin akan di rombak menjadi bilirubin dan biliverdin. Bilirubin dan biliverdin ini merupakan zat warna bagi empedu dan mengandung warna hijau-biru. Zat warna tersebut di dalam usus akan mengalami oksidasi menjadi urobilin. Urobilin kemudian di eksresikan dari dalam tubuh dan memberi warna kekuningan pada feses dan urine ...
Figure 3.1 Breakdown of haem moiety via biliverdin to bilirubin. Figure 3.2 Overview of excretion of bilirubin and its metabolism. It is the main by-product (via biliverdin) from the oxidation and breakdown of the haem moiety arising from red cell destruction (80%) and other proteins, such as myoglobin and catalase (20%), in the reticuloendothelial system…
Porphyrins are a accumulation of heterocyclic macrocycle amoebic compounds, composed of four adapted pyrrole subunits commutual at their α carbon atoms via methine bridges (=CH−). The ancestor porphyrin is porphin, and commissioned porphines are alleged porphyrins. The porphyrin ring anatomy is aromatic, with a absolute of 26 electrons in the conjugated system. Various analyses announce…
Pathways of intracellular communication: tetrapyrroles and plastid-to-nucleus signaling. Checkpoint signaling: epigenetic events sound the DNA strand-breaks alarm to the ATM proein kinase
Tomato Heme Oxygenase 1 antibody LS-C137028 is an unconjugated rabbit polyclonal antibody to tomato Tomato Heme Oxygenase 1. Validated for ELISA and WB.
Amlodipine dimethyl ester/ACM140171660 can be provided in Alfa Chemistry. We are dedicated to provide our customers the best products and services.
J R Hess Company is a leading supplier of dimethyl esters (also known as DMEs, dibasic esters and DBEs) and optimized co-solvent blends.
Photoconversion, the method by which a fluorescent dye is transformed into a stable, osmiophilic product that can be visualized by electron microscopy, is the most widely used method to enable the ultrastructural analysis of fluorescently labeled cellular structures
In studies in mice, Johns Hopkins Medicine researchers report they have found that bilirubin, a bile pigment most commonly known for yellowing the skin of people with jaundice, may play an unexpected role in protecting brain ...
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Heme oxygenase-1 (HO-1) is an inducible, detoxifying enzyme that is critical for limiting oxidative stress, inflammation, and cellular injury within the CNS and other tissues. Here, we demonstrate a deficiency of HO-1 expression in the brains of HIV-infected individuals. This HO-1 .... ...
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Also biliverdine was present, a bile component expected in the liver. The blood might also partly have originated from the ...
... biliverdine MeSH D03.383.129.578.840.249.727 - urobilin MeSH D03.383.129.578.840.249.852 - urobilinogen MeSH D03.383.129.578. ... biliverdine MeSH D03.549.909.249.727 - urobilin MeSH D03.549.909.249.852 - urobilinogen MeSH D03.549.909.374 - chlorophyll MeSH ...
... biliverdine MeSH D23.767.193.727 - urobilin MeSH D23.767.193.852 - urobilinogen MeSH D23.767.261.050 - beta carotene MeSH ...
... biliverdine MeSH D04.345.783.249.727 - urobilin MeSH D04.345.783.249.852 - urobilinogen MeSH D04.345.783.374 - chlorophyll MeSH ...
The bile of amphibia and of birds contains biliverdine only. Does not occur in normal human bile or normal human serum, but ...
Recentemente, estudos demonstraram que a indução da HO-1 ou a terapia com o CO e a biliverdina, isoladamente ou em associação, ... Nossa proposta foi estudar o efeito da modulação da HO-1 e do tratamento com a biliverdina em um modelo mais clinicamente ... O tratamento com a biliverdina também teve um impacto significativo, tanto em um modelo de endotoxemia letal como no modelo de ... RODRIGUES, P. M. de A. Heme oxigenase-1 como um alvo terapêutico na sepse o papel da biliverdina. 2007. 93f. Dissertação ( ...
BILIVERDINE IX ALPHA. C33 H34 N4 O6. GWZYPXHJIZCRAJ-SRVCBVSDSA-N. ...
Complete information for BLVRA gene (Protein Coding), Biliverdin Reductase A, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
DB02073 Biliverdine Ix Alpha. DB01942 Formic Acid. DB00157 NADH. DB04912 Stannsoporfin. DB04803 Verdoheme. DB00163 Vitamin E. ... DB02073 Biliverdine Ix Alpha. DB01942 Formic Acid. DB00157 NADH. DB04912 Stannsoporfin. DB04803 Verdoheme. DB00163 Vitamin E. ...
Biliverdine IX Alpha. experimental. unknown. Details. DB02396. Methylethylamine. experimental. unknown. Details. DB02528. ...
Also biliverdine was present, a bile component expected in the liver. The blood might also partly have originated from the ...
C-PHYCOCYANIN, PHYCOCYANOBILIN, BILIVERDINE IX ALPHA. Authors:. Satyanarayana, L., Patel, A., Mishra, S., K Ghosh, P., Suresh, ...
This patent search tool allows you not only to search the PCT database of about 2 million International Applications but also the worldwide patent collections. This search facility features: flexible search syntax; automatic word stemming and relevance ranking; as well as graphical results.
biliverdine (bili-verdin), A green bile pigment formed from the oxidation of heme; a bilin with a structure almost identical ...
Chrisman, I. M., Nemetchek, M. D., De Vera, I. M. S., Shang, J., Heidari, Z., Long, Y., Reyes-Caballero, H., Galindo-Murillo, R., Cheatham, T. E., Blayo, A. L., Shin, Y., Fuhrmann, J., Griffin, P. R., Kamenecka, T. M., Kojetin, D. J. & Hughes, T. S., Dec 1 2018, In : Nature Communications. 9, 1, 1794.. Research output: Contribution to journal › Article ...
Biliverdine Medicine & Life Sciences Schizophrenia Medicine & Life Sciences Bilirubin Medicine & Life Sciences ...
... biliverdine, bongkrekic acid, bumadizon, caffeic acid, calcium 2-ethylbutanoate, capobenic acid, carprofen, cefodizime, ...
Oxidarea hemului genereaza biliverdina, care este metabolizata la randul sau in bilirubina. Restul de 15-20% din bilirubina ...
... biliverdine MeSH D03.383.129.578.840.249.727 - urobilin MeSH D03.383.129.578.840.249.852 - urobilinogen MeSH D03.383.129.578. ... biliverdine MeSH D03.549.909.249.727 - urobilin MeSH D03.549.909.249.852 - urobilinogen MeSH D03.549.909.374 - chlorophyll MeSH ...
... debido a la liberación de un producto de degradación de la hemoglobina llamado biliverdina).. Los Streptococcus pneumonaie y ...
This patent search tool allows you not only to search the PCT database of about 2 million International Applications but also the worldwide patent collections. This search facility features: flexible search syntax; automatic word stemming and relevance ranking; as well as graphical results.
Biliverdine / blood. Cell Adhesion Molecules / biosynthesis. Cell Communication / drug effects. Cells, Cultured. Disease Models ...
vanadic acid to form biliverdine in serum,Then the absorbance of R-1 210 µL 210 µL 210 µL bilirubin at 450nm decreases and is ...
TY - JOUR. T1 - Clinical and experimental evidence for oxidative stress as an exacerbating factor of diabetes mellitus. AU - Takayanagi, Ryoichi. AU - Inoguchi, Toyoshi. AU - Ohnaka, Keizo. PY - 2011/1/1. Y1 - 2011/1/1. N2 - The involvement of reactive oxygen species in various diseases has been demonstrated almost in vitro or in animal studies and clinical studies supporting the involvement of reactive oxygen species are very few. Bilirubin has been recognized as an important antioxidant and also shown to have an inhibitory effect on the activity of NADPH oxidase, which may be an important source for superoxide production in various tissues. When the prevalence of vascular complcations was compared in diabetic patients with and without a congenital hyperbilirubinemia (Gilbert syndrome), the prevalence of retinopathy, macroalbuminuria and coronary artery disease in patients with Gilbert syndrome was about 20% of that in those without Gilbert syndrome. For study of lifestyle-related diseases, the ...
Bhagat, T. D., Chen, S., Bartenstein, M., Barlowe, A. T., Von Ahrens, D., Choudhary, G. S., Tivnan, P., Amin, E., Marcondes, A. M., Sanders, M. A., Hoogenboezem, R. M., Kambhampati, S., Ramachandra, N., Mantzaris, I., Sukrithan, V., Laurence, R., Lopez, R., Bhagat, P., Giricz, O., Sohal, D. & 18 others, Wickrema, A., Yeung, C., Gritsman, K., Aplan, P., Hochedlinger, K., Yu, Y., Pradhan, K., Zhang, J., Greally, J. M., Mukherjee, S., Pellagatti, A., Boultwood, J., Will, B., Steidl, U., Raaijmakers, M. H. G. P., Deeg, H. J., Kharas, M. G. & Verma, A., Sep 15 2017, In : Cancer Research. 77, 18, p. 4846-4857 12 p.. Research output: Contribution to journal › Article ...
TY - JOUR. T1 - Biochemical and structural characterization of Pseudomonas aeruginosa Bfd and FPR. T2 - Ferredoxin NADP+ reductase and not ferredoxin is the redox partner of heme oxygenase under iron-starvation conditions. AU - Wang, An. AU - Zeng, Yuhong. AU - Han, Huijong. AU - Weeratunga, Saroja. AU - Morgan, Bailey N.. AU - Moenne-Loccoz, Pierre. AU - Schönbrunn, Ernst. AU - Rivera, Mario. PY - 2007/10/30. Y1 - 2007/10/30. N2 - Among the 118 genes upregulated by Pseudomonas aeruginosa in response to iron starvation [Ochsner, U. A., Wilderman, P. J., Vasil, A. I., and Vasil, M. L. (2002) Mol. Microbiol. 45, 1277-1287], we focused on the products of the two genes encoding electron transfer proteins, as a means of identifying the redox partners of the heme oxygenase (pa-HO) expressed under low-iron stress conditions. Biochemical and spectroscopic investigations demonstrated that the bfd gene encodes a 73-amino acid protein (pa-Bfd) that incorporates a [2Fe-2S]2+/+ center, whereas the fpr gene ...
TY - JOUR. T1 - Identification and Functional Characterization of Bilitranslocase in Sea-Bass (Dicentrarchus labrax) Hepatopancreas. AU - Delneri, A.. AU - Franca, R.. AU - Terdoslavich, M.. AU - Montanič, S.. AU - Čurin Šerbec, V.. AU - Tramer, F.. AU - Francese, M.. AU - Passamonti, S.. PY - 2011/12. Y1 - 2011/12. N2 - The mammalian bilirubin transporter bilitranslocase (BTL, T.C.#2.A.65.1.1) is found in both absorptive (intestine) and excretory epithelia (liver, kidney) and in the vascular endothelium. The aim of this work was to investigate whether a BTL homologue is expressed also in fish hepatopancreas. Immunochemistry based on an antisequence antibody specific for rat liver BTL demonstrated the presence of such homologue in sea-bass (Dicentrarchus labrax) hepatopancreas. Furthermore the transport activity of such a carrier, measured as electrogenic bromosulphophthalein (BSP) uptake, was assayed in sea-bass microsomes, where it was inhibited by the same antibody. Transport activity in ...
La HO es la enzima responsable de degradar el grupo hemo, liberando biliverdina, Fe2+ y monóxido de carbono71, los cuales son ...
TY - JOUR. T1 - Heme oxygenase-1 is induced in glia throughout brain by subarachnoid hemoglobin. AU - Turner, Christopher P.. AU - Bergeron, Marcelle. AU - Matz, Paul. AU - Zegna, Angelo. AU - Noble, Linda J.. AU - Panter, S. Scott. AU - Sharp, Frank R. PY - 1998/3. Y1 - 1998/3. N2 - The heme oxygenase-1 gene, HO-1, induced by heme, ischemia, and heat shock, metabolizes heme to biliverdin, free iron, and carbon monoxide. Though the distribution of HO-1 has been described in normal rat brain, little is known about how extracellular heme proteins in the subarachnoid space distribute in brain. To address this issue, hemoglobin was injected into the cisterna magna of adult rats. Expression of HO-1 in these animals was compared with saline-injected, BSA-injected, and uninjected controls. Western blot analysis showed that 24 hours after injection oxyhemoglobin increased HO-1 levels approximately four- to fivefold in all brain regions studied compared with saline-injected and BSA-injected controls. In ...
... geralmente biliverdina. ─ γ-hemolítico: γ-hemolítico hemolisinas) não tem hemólise (ausência de ...
Biliverdine Medicine & Life Sciences Bryopsida Medicine & Life Sciences Eschscholzia Medicine & Life Sciences ...
  • I found quite a lot of work which links bilirubin and bile salts, for example www.revision-notes.co.uk/revision/859.html , in describing the process of bile secretion, states of bile "It is an alkaline, mucous fluid containing bile pigments, biliverdine and bilirubin. (gilbertssyndrome.org.uk)
  • A heme oxigenase-1 (HO-1), uma enzima induzida sob diversas condições de estresse celular, cataboliza o heme em monóxido de carbono (CO), biliverdina (convertida posteriormente a bilirrubina) e ferro livre. (fiocruz.br)
  • Nessa tese, nós demonstramos que epimastigotas cultivados com heme, produziram os compostos, α-meso hidroxiheme, verdoheme e biliverdina (identificados por HPLC acoplado á espectrofotômetria). (bvsalud.org)
  • Heme oxygenase catalyzes the metabolism of heme to biliverdine, free iron, and carbon monoxide. (faintpower.ml)
  • The bile of amphibia and of birds contains biliverdine only. (drugfuture.com)
  • The Research Group Toxicology and Ecotoxicology Wildlife of the Instituto de Investigación en Recursos Cinegéticos (IREC - CSIC, UCLM, JCCM) It is created in mid-2003 and since then has worked in the exposure assessment to different types of toxic wildlife And to study the effects they can have on the individual and the conservation of stocks. (irec.es)