Selenious Acid
Selenium
Organoselenium Compounds
Sodium Selenite
Selenium Radioisotopes
Glutathione Peroxidase
Selenocysteine
Cystine
Ethionine
Radioisotopes
Crystallization
Crystallography, X-Ray
Plant Poisoning
The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds. (1/305)
The molybdate-dependent transcriptional regulator (ModE) from Escherichia coli functions as a sensor of molybdate concentration and a regulator for transcription of operons involved in the uptake and utilization of the essential element, molybdenum. We have determined the structure of ModE using multi-wavelength anomalous dispersion. Selenomethionyl and native ModE models are refined to 1. 75 and 2.1 A, respectively and describe the architecture and structural detail of a complete transcriptional regulator. ModE is a homodimer and each subunit comprises N- and C-terminal domains. The N-terminal domain carries a winged helix-turn-helix motif for binding to DNA and is primarily responsible for ModE dimerization. The C-terminal domain contains the molybdate-binding site and residues implicated in binding the oxyanion are identified. This domain is divided into sub-domains a and b which have similar folds, although the organization of secondary structure elements varies. The sub-domain fold is related to the oligomer binding-fold and similar to that of the subunits of several toxins which are involved in extensive protein-protein interactions. This suggests a role for the C-terminal domain in the formation of the ModE-protein-DNA complexes necessary to regulate transcription. Modelling of ModE interacting with DNA suggests that a large distortion of DNA is not necessary for complex formation. (+info)The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome. (2/305)
Ribosomal protein L2 is the largest protein component in the ribosome. It is located at or near the peptidyl transferase center and has been a prime candidate for the peptidyl transferase activity. It binds directly to 23S rRNA and plays a crucial role in its assembly. The three-dimensional structure of the RNA-binding domain of L2 from Bacillus stearothermophilus has been determined at 2.3 A resolution by X-ray crystallography using the selenomethionyl MAD method. The RNA-binding domain of L2 consists of two recurring motifs of approximately 70 residues each. The N-terminal domain (positions 60-130) is homologous to the OB-fold, and the C-terminal domain (positions 131-201) is homologous to the SH3-like barrel. Residues Arg86 and Arg155, which have been identified by mutation experiments to be involved in the 23S rRNA binding, are located at the gate of the interface region between the two domains. The molecular architecture suggests how this important protein has evolved from the ancient nucleic acid-binding proteins to create a 23S rRNA-binding domain in the very remote past. (+info)Crystal structure of the human O(6)-alkylguanine-DNA alkyltransferase. (3/305)
The mutagenic and carcinogenic effects of simple alkylating agents are mainly due to O(6)-alkylation of guanine in DNA. This lesion results in transition mutations. In both prokaryotic and eukaryotic cells, repair is effected by direct reversal of the damage by a suicide protein, O(6)-alkylguanine-DNA alkyltransferase. The alkyltransferase removes the alkyl group to one of its own cysteine residues. However, this mechanism for preserving genomic integrity limits the effectiveness of certain alkylating anticancer agents. A high level of the alkyltransferase in many tumour cells renders them resistant to such drugs. Here we report the X-ray structure of the human alkyltransferase solved using the technique of multiple wavelength anomalous dispersion. This structure explains the markedly different specificities towards various O(6)-alkyl lesions and inhibitors when compared with the Escherichia coli protein (for which the structure has already been determined). It is also used to interpret the behaviour of certain mutant alkyltransferases to enhance biochemical understanding of the protein. Further examination of the various models proposed for DNA binding is also permitted. This structure may be useful for the design and refinement of drugs as chemoenhancers of alkylating agent chemotherapy. (+info)Structural interactions of fibroblast growth factor receptor with its ligands. (4/305)
Fibroblast growth factors (FGFs) effect cellular responses by binding to FGF receptors (FGFRs). FGF bound to extracellular domains on the FGFR in the presence of heparin activates the cytoplasmic receptor tyrosine kinase through autophosphorylation. We have crystallized a complex between human FGF1 and a two-domain extracellular fragment of human FGFR2. The crystal structure, determined by multiwavelength anomalous diffraction analysis of the selenomethionyl protein, is a dimeric assemblage of 1:1 ligand:receptor complexes. FGF is bound at the junction between the two domains of one FGFR, and two such units are associated through receptor:receptor and secondary ligand:receptor interfaces. Sulfate ion positions appear to mark the course of heparin binding between FGF molecules through a basic region on receptor D2 domains. This dimeric assemblage provides a structural mechanism for FGF signal transduction. (+info)Adaptive responses and apoptosis in endothelial cells exposed to carbon monoxide. (5/305)
Prior studies have shown that exposure to carbon monoxide (CO) will elevate the steady-state concentration of nitric oxide ((.)NO) in several cell types and body organs and that some toxic effects of CO are directed toward endothelial cells. Studies reported in this paper were conducted with bovine pulmonary artery endothelial cells exposed to 10 to 100 ppm CO to achieve concentrations between 11 and 110 nM in air-saturated buffer. Exposure to 11 nM CO increased synthesis of manganous superoxide dismutase and conferred resistance against the lethal effects of 110 nM CO. At concentrations of 88 nM CO or more, exposures for 1 h or longer caused cell death that became apparent 18 h after the exposure ceased. Caspase-1 was activated in response to CO, and cell death was inhibited by a caspase-1 inhibitor. Alteration of proteolytic pathways by CO was indicated by the presence of ubiquitin-containing intracellular inclusion bodies. Morphological changes and caspase activation indicated that cell death was an apoptotic process. Cells exposed to 110 nM CO had higher concentrations of manganous superoxide dismutase and heme oxygenase-1 but no changes in glutathione peroxidase, glucose-6-phosphate dehydrogenase, thiols, or catalase. Elevated levels of antioxidant enzymes and apoptosis were inhibited by the nitric oxide synthase inhibitor, S-isopropylisothiourea, and the peroxynitrite scavenger, selenomethionine. These results show that biochemical effects of CO occur at environmentally relevant concentrations, that apoptotic cell death follows exposure to relatively high concentrations of CO, and that these actions of CO are mediated by nitric oxide. (+info)Effects of organic and inorganic selenium supplementation on selenoenzyme activity in blood lymphocytes, granulocytes, platelets and erythrocytes. (6/305)
The blood selenium (Se) concentration in the U.K. population has declined by approx. 50% between 1974 and 1991, reflecting a large decrease in dietary Se supply, with intakes only half the reference nutrient intake of 1 microg/kg body weight. Tissue levels of Se are readily influenced by dietary intake. Therefore selenoprotein activity may be sub-optimal due to low Se status, and thus compromise normal cell function. To examine the effects of changing Se intake on selenoproteins, we have determined the relative effectiveness of organic selenomethionine and inorganic sodium selenite (50 microg of Se daily for 28 days) in modulating glutathione peroxidase activities in blood cells from 45 healthy men and women, from a U.K. population. Transient and acute changes in lymphocyte, granulocyte and platelet phospholipid-hydroperoxide glutathione peroxidase (GPx4) activity occurred by day 7 or 14 of sodium selenite treatment and by day 7 in lymphocytes from selenomethionine-treated subjects compared with controls taking a placebo. In contrast, GPx4 activity in granulocytes and platelets in the selenomethionine group increased gradually over the 28 days. Cytosolic glutathione peroxidase (GPx1) activity in these blood cells from both treatment groups increased gradually over the 28 days. For each cellular selenoenzyme activity a significant inter-individual difference (P<0.001) in the extent of the response to Se supplementation was observed, but this was not related to blood Se concentrations either before or after treatments. Significant inverse correlations were evident between baseline enzyme activities and percentage change in activity after 28 days of supplementation [e.g. lymphocyte GPx4, r=-0.695 (P<0.001)], indicating that pre-treatment activity may be sub-optimal as a result of poor Se status. The different and contrasting effects that Se supplementation had on blood selenoenzyme activities may be indicative of a difference in metabolic need for Se regulated at the level of Se-dependent cell function. (+info)Selenomethionine: a review of its nutritional significance, metabolism and toxicity. (7/305)
Although the need for selenium in human and animal nutrition is well recognized, the question concerning the proper form of selenium for supplemental use is still being debated. Ideally, selenium should be supplemented in the form in which it occurs naturally in foods. Because the L-isomer of selenomethionine (Se-met) is a major natural food-form of selenium, synthetic L-Se-met or enriched food sources thereof such as selenium yeast are appropriate supplemental forms of Se for humans; for animals, DL-Se-met is acceptable. Ingested Se-met is either metabolized directly to reactive forms of selenium or stored in place of methionine in body proteins. Se-met metabolism is closely linked to protein turnover. At constant intakes in the nutritional range, tissue Se levels increase until a steady state is established, preventing the build-up to toxic levels. (+info)Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism. (8/305)
Carbon-carbon bond formation is an essential reaction in organic chemistry and the use of aldolase enzymes for the stereochemical control of such reactions is an attractive alternative to conventional chemical methods. Here we describe the crystal structures of a novel class II enzyme, 2-dehydro-3-deoxy-galactarate (DDG) aldolase from Escherichia coli, in the presence and absence of substrate. The crystal structure was determined by locating only four Se sites to obtain phases for 506 protein residues. The protomer displays a modified (alpha/beta)(8) barrel fold, in which the eighth alpha-helix points away from the beta-barrel instead of packing against it. Analysis of the DDG aldolase crystal structures suggests a novel aldolase mechanism in which a phosphate anion accepts the proton from the methyl group of pyruvate. (+info)Selenomethionine is an organic form of selenium, which is an essential trace element in human nutrition. It is incorporated into proteins in place of methionine, one of the 20 standard amino acids, and functions as an antioxidant by helping to prevent cellular damage from free radicals. Selenomethionine can be found in a variety of foods, including brazil nuts, fish, meat, and whole grains, and is also available as a dietary supplement.
Selenious acid, also known as selenic acid or hydrogen selenite, is not a substance that has a widely accepted medical definition. However, it is a chemical compound with the formula H2SeO3. It is a colorless, odorless liquid that is used in some industrial processes and is highly toxic if ingested or inhaled.
In the context of human health, selenium is an essential trace element that plays a critical role in various biological processes, including antioxidant defense systems, thyroid hormone metabolism, and immune function. Selenium can be found in various forms, including selenomethionine, selenocysteine, and selenite.
Selenious acid is not a form of selenium that is typically used or encountered in medical or nutritional contexts. However, it is possible that small amounts of selenious acid may be produced as an intermediate during the metabolism of certain selenium compounds in the body.
Selenium is a trace element that is essential for the proper functioning of the human body. According to the medical definitions provided by the National Institutes of Health (NIH), selenium is a component of several major metabolic pathways, including thyroid hormone metabolism, antioxidant defense systems, and immune function.
Selenium is found in a variety of foods, including nuts (particularly Brazil nuts), cereals, fish, and meat. It exists in several forms, with selenomethionine being the most common form found in food. Other forms include selenocysteine, which is incorporated into proteins, and selenite and selenate, which are inorganic forms of selenium.
The recommended dietary allowance (RDA) for selenium is 55 micrograms per day for adults. While selenium deficiency is rare, chronic selenium deficiency can lead to conditions such as Keshan disease, a type of cardiomyopathy, and Kaschin-Beck disease, which affects the bones and joints.
It's important to note that while selenium is essential for health, excessive intake can be harmful. High levels of selenium can cause symptoms such as nausea, vomiting, hair loss, and neurological damage. The tolerable upper intake level (UL) for selenium is 400 micrograms per day for adults.
Organoselenium compounds are organic chemicals that contain selenium, a naturally occurring non-metal element, in their structure. Selenium is chemically related to sulfur and can replace it in many organic molecules. Organoselenium compounds have been studied for their potential therapeutic benefits, including antioxidant, anti-cancer, and anti-inflammatory effects. They are also used as catalysts in chemical reactions. These compounds contain at least one carbon atom bonded to selenium, which can take the form of a variety of functional groups such as selenoethers, selenols, and selenoesters.
Sodium Selenite is not a medical term per se, but it is a chemical compound with the formula Na2SeO3. It is used in medicine as a dietary supplement and also in veterinary medicine. Medically, it is used to treat selenium deficiency, which is rare.
Selenium is an essential trace element for human health, playing a crucial role in various physiological processes, such as antioxidant defense systems, thyroid hormone metabolism, and DNA synthesis. Sodium Selenite serves as a source of selenium in these medical applications.
Please note that supplementation with sodium selenite should be under the supervision of a healthcare professional, as excessive selenium intake can lead to selenosis, a condition characterized by symptoms like nausea, vomiting, hair loss, and neurological damage.
Selenium radioisotopes are unstable forms of the element selenium that emit radiation as they decay into more stable forms. These isotopes can be produced through various nuclear reactions, such as irradiating a stable selenium target with protons or alpha particles. Some examples of selenium radioisotopes include selenium-75, selenium-79, and selenium-81.
Selenium-75 is commonly used in medical imaging to study the function of the thyroid gland, as it accumulates in this gland and can be detected using a gamma camera. Selenium-79 and selenium-81 have potential uses in cancer treatment, as they can be incorporated into compounds that selectively target and destroy cancer cells. However, more research is needed to fully understand the potential benefits and risks of using these radioisotopes in medical treatments.
It's important to note that handling and using radioisotopes requires special training and precautions, as they can be dangerous if not handled properly. Exposure to radiation from radioisotopes can increase the risk of cancer and other health problems, so it's essential to use them only under controlled conditions and with appropriate safety measures in place.
Glutathione peroxidase (GPx) is a family of enzymes with peroxidase activity whose main function is to protect the organism from oxidative damage. They catalyze the reduction of hydrogen peroxide, lipid peroxides, and organic hydroperoxides to water or corresponding alcohols, using glutathione (GSH) as a reducing agent, which is converted to its oxidized form (GSSG). There are several isoforms of GPx found in different tissues, including GPx1 (also known as cellular GPx), GPx2 (gastrointestinal GPx), GPx3 (plasma GPx), GPx4 (also known as phospholipid hydroperoxide GPx), and GPx5-GPx8. These enzymes play crucial roles in various biological processes, such as antioxidant defense, cell signaling, and apoptosis regulation.
I'm sorry for any confusion, but "Fish Flour" is not a recognized term in medical terminology. It is possible that you may be referring to "fish meal," which is a product made from ground-up fish and is used as a protein source in animal feeds. However, it is not typically used in human food or medicine. If you have any concerns about the use of this substance or any other unusual substances in human health, I would recommend consulting with a healthcare professional for accurate information.
Methionine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. It plays a crucial role in various biological processes, including:
1. Protein synthesis: Methionine is one of the building blocks of proteins, helping to create new proteins and maintain the structure and function of cells.
2. Methylation: Methionine serves as a methyl group donor in various biochemical reactions, which are essential for DNA synthesis, gene regulation, and neurotransmitter production.
3. Antioxidant defense: Methionine can be converted to cysteine, which is involved in the formation of glutathione, a potent antioxidant that helps protect cells from oxidative damage.
4. Homocysteine metabolism: Methionine is involved in the conversion of homocysteine back to methionine through a process called remethylation, which is essential for maintaining normal homocysteine levels and preventing cardiovascular disease.
5. Fat metabolism: Methionine helps facilitate the breakdown and metabolism of fats in the body.
Foods rich in methionine include meat, fish, dairy products, eggs, and some nuts and seeds.
Selenocysteine (Sec) is a rare, naturally occurring amino acid that contains selenium. It is encoded by the opal (TGA) codon, which typically signals stop translation in mRNA. However, when followed by a specific hairpin-like structure called the Sec insertion sequence (SECIS) element in the 3' untranslated region of the mRNA, the TGA codon is interpreted as a signal for selenocysteine incorporation during protein synthesis.
Selenocysteine plays an essential role in several enzymes involved in antioxidant defense and redox homeostasis, such as glutathione peroxidases, thioredoxin reductases, and iodothyronine deiodinases. These enzymes require selenocysteine for their catalytic activity due to its unique chemical properties, which allow them to neutralize harmful reactive oxygen species (ROS) and maintain proper cellular function.
In summary, selenocysteine is a specialized amino acid containing selenium that is encoded by the TGA codon in mRNA when accompanied by a SECIS element. It is crucial for the activity of several enzymes involved in antioxidant defense and redox homeostasis.
Cystine is a naturally occurring amino acid in the body, which is formed from the oxidation of two cysteine molecules. It is a non-essential amino acid, meaning that it can be produced by the body and does not need to be obtained through diet. Cystine plays important roles in various biological processes, including protein structure and antioxidant defense. However, when cystine accumulates in large amounts, it can form crystals or stones, leading to conditions such as cystinuria, a genetic disorder characterized by the formation of cystine kidney stones.
Selenium compounds refer to chemical substances that contain the metalloid element selenium (Se) in its various oxidation states, combined with other elements. These compounds can be organic or inorganic and can exist in different forms, such as selenides, selenites, and selenates. Selenium is an essential trace element for human health, playing a crucial role in several biological processes, including antioxidant defense, immune function, and thyroid hormone metabolism. However, excessive exposure to certain selenium compounds can be toxic and cause serious health effects.
Ethionine is a toxic, synthetic analog of the amino acid methionine. It is an antimetabolite that inhibits the enzyme methionine adenosyltransferase, which plays a crucial role in methionine metabolism. Ethionine is often used in research to study the effects of methionine deficiency and to create animal models of various human diseases. It is not a natural component of human nutrition and has no known medical uses. Prolonged exposure or high levels of ethionine can lead to liver damage, growth impairment, and other harmful health effects.
Radioisotopes, also known as radioactive isotopes or radionuclides, are variants of chemical elements that have unstable nuclei and emit radiation in the form of alpha particles, beta particles, gamma rays, or conversion electrons. These isotopes are formed when an element's nucleus undergoes natural or artificial radioactive decay.
Radioisotopes can be produced through various processes, including nuclear fission, nuclear fusion, and particle bombardment in a cyclotron or other types of particle accelerators. They have a wide range of applications in medicine, industry, agriculture, research, and energy production. In the medical field, radioisotopes are used for diagnostic imaging, radiation therapy, and in the labeling of molecules for research purposes.
It is important to note that handling and using radioisotopes requires proper training, safety measures, and regulatory compliance due to their ionizing radiation properties, which can pose potential health risks if not handled correctly.
Crystallization is a process in which a substance transitions from a liquid or dissolved state to a solid state, forming a crystal lattice. In the medical context, crystallization can refer to the formation of crystals within the body, which can occur under certain conditions such as changes in pH, temperature, or concentration of solutes. These crystals can deposit in various tissues and organs, leading to the formation of crystal-induced diseases or disorders.
For example, in patients with gout, uric acid crystals can accumulate in joints, causing inflammation, pain, and swelling. Similarly, in nephrolithiasis (kidney stones), minerals in the urine can crystallize and form stones that can obstruct the urinary tract. Crystallization can also occur in other medical contexts, such as in the formation of dental calculus or plaque, and in the development of cataracts in the eye.
X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.
Plant poisoning is a form of poisoning that occurs when someone ingests, inhales, or comes into contact with any part of a plant that contains toxic substances. These toxins can cause a range of symptoms, depending on the type and amount of plant consumed or exposed to, as well as the individual's age, health status, and sensitivity to the toxin.
Symptoms of plant poisoning may include nausea, vomiting, diarrhea, abdominal pain, difficulty breathing, skin rashes, seizures, or in severe cases, even death. Some common plants that can cause poisoning include poison ivy, poison oak, foxglove, oleander, and hemlock, among many others.
If you suspect plant poisoning, it is important to seek medical attention immediately and bring a sample of the plant or information about its identity if possible. This will help healthcare providers diagnose and treat the poisoning more effectively.
Selenoproteins are a specific group of proteins that contain the essential micronutrient selenium in the form of selenocysteine (Sec), which is a naturally occurring amino acid. Selenocysteine is encoded by the opal codon UGA, which typically serves as a stop codon in mRNA.
There are 25 known human selenoproteins, and they play crucial roles in various physiological processes, including antioxidant defense, DNA synthesis, thyroid hormone metabolism, and immune function. Some of the well-known selenoproteins include glutathione peroxidases (GPxs), thioredoxin reductases (TrxRs), and iodothyronine deiodinases (IDIs).
The presence of selenocysteine in these proteins makes them particularly efficient at catalyzing redox reactions, which involve the gain or loss of electrons. This property is essential for their functions as antioxidants and regulators of cellular signaling pathways.
Deficiencies in selenium can lead to impaired function of selenoproteins, potentially resulting in various health issues, such as increased oxidative stress, weakened immune response, and disrupted thyroid hormone metabolism.
Selenomethionine
Amino acid
Selenide
Selenium yeast
Vitamin B6
Methylselenocysteine
Non-proteinogenic amino acids
Carbon disulfide hydrolase
Marion Robinson
Cat food
Selenium in biology
Selenium
Selenium compounds
Selenoprotein
Selenocysteine
Selenium deficiency
Sum activity of peripheral deiodinases
Lecythis minor
Thyroid's secretory capacity
Methaneseleninic acid
NS2-3 protease
Chalcogen
Organoselenium chemistry
Glucose-6-phosphate dehydrogenase (coenzyme-F420)
Keshan disease
Single-wavelength anomalous dispersion
Nediljko Budisa
Fluorinase
Intelectin
Facioscapulohumeral muscular dystrophy
Selenomethionine - Wikipedia
Pure Encapsulations Selenium - selenomethionine -- 60 Capsules - Vitacost
Selenomethionine supplementation reduces lesion burden, improves
RCSB PDB - 2E1V: Crystal structure of Dendranthema morifolium DmAT, seleno-methionine derivative
IUCr) XANES measurements of the rate of radiation damage to selenome-thionine side chains
Long-term supplementation with selenate and selenomethionine: Selenium and glutathione peroxidase (EC 1.11.1.9) in blood...
Transcriptome-based exploration of potential molecular targets and mechanisms of selenomethionine in alleviating renal ischemia...
Selenium 100 mcg by New Roots Herbal | From Yeast-Free ʟ-Selenomethionine Antioxidant (100 capsules) | Natural Health...
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Selenomethionine 100y Tabl 120 1909 Metagenics - PharmaMedical
Preferred Nutrition Selenomethionine 200mcg 60 Veggie Caps - Essence of Life Organics
Buy Selenium (L-Selenomethionine) Powder Online in the UK | Customized Bends
"Pro- and Antioxidant Activity of Selenomethionine: Preventative Measur" by Austin Mroz
EUR-Lex - 02002L0046-20210330 - EN - EUR-Lex
ThyroNourish | Natural Thyroid Health
Superior in vivo inhibitory efficacy of methylseleninic acid against human prostate cancer over selenomethionine or selenite<...
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L-Metionina European Pharmacopoeia (EP) Reference Standard | Sigma-Aldrich
IUCr) Crystal structure of the putative cyclase IdmH from the indanomycin nonribosomal peptide synthase/polyketide synthase
SeMet5
- Selenomethionine (SeMet) is a naturally occurring amino acid. (wikipedia.org)
- Selenomethionine (SeMet) is an organic form of selenium (Se), an essential trace element that functions in the regulation of the immune response by both bolstering the endogenous thioredoxin and glutathione antioxidant defence systems and by directly scavenging damaging oxidant species. (greenmedinfo.com)
- This study aims toelucidate the effects of selenomethionine (SeMet) on DNA damage mediated by Cu(II),Fe(II), or Cr(III) metal ions. (rose-hulman.edu)
- Here, we evaluated the growth inhibitory effects of two presumed methylselenol precursors methylseleninic acid (MSeA) and Se-methylselenocysteine (MSeC) in comparison with selenomethionine (SeMet) and selenite in DU145 and PC-3 human PCa xenografts in athymic nude mice. (umn.edu)
- Hydroxy-selenomethionine (OH-SeMet) is a commercial organic source that has not been thoroughly evaluated as a single supplemental source of Se. (ifiscollections.org)
Biotics Research1
- Home / DIETARY SUPPLEMENTS / Biotics Research / Selenomethionine High Potency Selenium, Reproduction, Thyroid Gland Function, DNA Production, Cognitive Health, Potent Antioxidant. (drosolutions.com)
Hydroxy-selenomethionine2
- Feedinfo News Service recently spoke to Dr. Pierre-André Geraert, Adisseo's Director Scientific Marketing to get a better understanding of the role organic selenium can play in animal nutrition and health and how beneficial hydroxy-selenomethionine really is. (adisseo.com)
- Broiler meat production as affected by dietary supplemental hydroxy-selenomethionine. (ifiscollections.org)
Bound to methionine3
- Some research suggests that the inorganic form, selenite, is harder for the body to absorb than organic forms such as selenomethionine (selenium bound to methionine, an essential amino acid) or high-selenium yeast (which contains selenomethionine). (wikipedia.org)
- Thorne's Selenomethionine uses the purest form of selenium - bound to methionine for optimal absorption - without adding unnecessary additives or preservatives. (vitahealthapothecary.com)
- L-selenomethionine, are selenium bound to methionine, an essential amino acid. (essenceoflifeorganics.com)
Supplementation4
- These data highlight the potential beneficial effect of selenomethionine supplementation as a therapeutic strategy for atherosclerosis. (greenmedinfo.com)
- Selenomethionine supplementation reduces lesion burden, improves vessel function and modulates the inflammatory response within the setting of atherosclerosis. (greenmedinfo.com)
- L-selenomethionine supplementation causes a significant decrease in ant-thyroid peroxidase levels in patients with Hashimoto's disease. (greenmedinfo.com)
- Supplementation with selenium-enriched yeast in the Nutritional Prevention of Cancer (NPC) trial reduced the incidence of prostate cancer by 52-65%, but the Selenium and Vitamin E Cancer Prevention Trial (SELECT) used selenomethionine supplements with or without vitamin E and was discontinued after 5.5 years when no benefit was seen in terms of prostate cancer risk reduction. (zrtlab.com)
Yeast2
- Thirty-three New Zealand women aged 18-23 years received daily for 32 weeks, 200 μg Se as Seenriched yeast (selenomethionine), or brewer's yeast mixed with selenate, or no added Se (placebo) in a double-blind trial. (cambridge.org)
- Selenomethionine exists in all eukaryotes, ranging from yeast to humans. (cymbiotika.ca)
Methionine9
- In vivo, selenomethionine is randomly incorporated instead of methionine. (wikipedia.org)
- Selenium and sulfur are chalcogens that share many chemical properties so the substitution of methionine with selenomethionine may have only a limited effect on protein structure and function. (wikipedia.org)
- Incorporation of selenomethionine into proteins in place of methionine aids the structure elucidation of proteins by X-ray crystallography using single- or multi-wavelength anomalous diffraction (SAD or MAD). (wikipedia.org)
- 2) Selenomethionine is a selenoamino acid that is the selenium analogue of methionine. (cymbiotika.ca)
- When you consume selenomethionine supplements, your body recognizes the selenium as the amino acid methionine and immediately incorporates it into its protein stores. (cymbiotika.ca)
- Determination of methionine and selenomethionine in food matrices by gas chromatography mass spectrometry after aqueous derivatization with triethyloxonium salts. (bvsalud.org)
- A novel analytical method for the simultaneous gas chromatography-mass spectrometry (GC-MS) determination of methionine and selenomethionine in food samples is described. (bvsalud.org)
- When analysis of a 1 mL volume of aqueous standard was performed, detection limits of 1 ng/g methionine and 10 ng/g for selenomethionine were obtained. (bvsalud.org)
- It uses the same active transport mechanism as for methionine, one of the 9 essential amino acids that can only be obtained from the diet, and this increases the efficiency of absorption of selenomethionine over inorganic forms of selenium. (zrtlab.com)
Incorporation3
- However, the incorporation of selenomethionine into tissue proteins and keratin in cattle, birds, and fish causes alkali disease. (wikipedia.org)
- 1991) are consistent with the incorporation of Se from selenomethionine into a general tissue protein pool while selenate is directly available for GSHPx synthesis, and explain the poorer correlation between Se and GSHPx in individuals with higher Se status. (cambridge.org)
- Dawson, P. E. Post-translational backbone engineering through selenomethionine-mediated incorporation of Freidinger lactams. (scripps.edu)
Easily absorbed2
- Although all selenium supplements are thought to produce similar effects in the body, selenomethionine is more easily absorbed than non-organic forms of selenium such as selenate. (cymbiotika.ca)
- L-selenomethionine is easily absorbed in the gastrointestinal tract and is better absorbed and retained in the body than other forms including selenite or selenate. (essenceoflifeorganics.com)
Selenite5
- It has been suggested by nutritionists that selenomethionine, as an organic form of selenium, is easier for the human body to absorb than selenite, which is an inorganic form. (wikipedia.org)
- It was determined in a clinical trial that selenomethionine is absorbed 19% better than selenite. (wikipedia.org)
- J 2008, ' Superior in vivo inhibitory efficacy of methylseleninic acid against human prostate cancer over selenomethionine or selenite ', Carcinogenesis , vol. 29, no. 5, pp. 1005-1012. (umn.edu)
- There was no effect after the same incubation period with concentrations of up to 0.03 millimoles of selenomethionine (1464422), but with concentrations as low as 0.0125 millimoles of sodium-selenite (10102188) there was significant toxicity to the cells. (cdc.gov)
- Selenomethionine and sodium selenite did not provide any protective action against the cellular disruption induced by Hg(2+) salt. (cdc.gov)
Human prostate1
- Selenomethionine has been found in human prostate, kidney and pancreas tissues, and has also been detected in multiple biofluids, such as urine and blood. (cymbiotika.ca)
Absorption1
- All forms of selenium are well absorbed, but absorption of selenomethionine is the best. (zrtlab.com)
Supplements1
- In fact, taking selenomethionine supplements results in plasma selenium stores twice as high as equivalent doses of non-organic selenium supplements such as selenate, according to the Natural Medicines Comprehensive Database. (cymbiotika.ca)
Acid1
- It is a member of selenomethionine and a selenoamino acid. (cymbiotika.ca)
Selenate2
- Selenomethionine was more effective in raising blood Se concentrations than selenate, but both were equally effective in raising GSHPx activities in whole blood, erythrocytes and plasma, indicating a similar bioavailability for the two forms. (cambridge.org)
- However, selenate raised platelet GSHPx activities to a greater extent than did selenomethionine suggesting some other effect of selenate on platelets which needs further investigation. (cambridge.org)
Form4
- The L-selenomethionine enantiomer is the main form of selenium found in Brazil nuts, cereal grains, soybeans, and grassland legumes, while Se-methylselenocysteine, or its γ-glutamyl derivative, is the major form of selenium found in Astragalus, Allium, and Brassica species. (wikipedia.org)
- Selenomethionine serves as a storage form of selenium. (vitacost.com)
- Selenomethionine, an organic form of selenium, is a readily absorbable form of this essential trace mineral. (livinghealthychoice.com)
- Here, the crystal structure of a selenomethionine-labelled truncated form of IdmH (IdmH- Δ 99-107) was solved using single-wavelength anomalous dispersion (SAD) phasing. (iucr.org)
Readily2
- Selenomethionine is readily oxidized. (wikipedia.org)
- Selenomethionine is readily available as a dietary supplement. (wikipedia.org)
Nutrition1
- Patients receiving long-term total parenteral nutrition have developed selenium deficiency with muscle pain and tenderness that responded to a selenomethionine supplement. (msdmanuals.com)
Water1
- Selenomethionine exists as a solid, soluble (in water), and a moderately acidic compound (based on its pKa). (cymbiotika.ca)
Amino acid2
- As a seleno amino acid, L-selenomethionine candirectly participate protein synthesis and largely deposited in tissues protein, so it has a high depositionrate in animal products(meat, egg, milk). (track4win.com)
- Selenomethionine (MSe) may be introduced as alternative label, which, due to its small size and amino acid nature, likely results in minimal alterations of the peptide physicochemical properties. (ku.dk)
Dietary supplement1
- Selenomethionine is readily available as a dietary supplement. (wikipedia.org)
Celecoxib3
- We conducted a randomized, controlled trial of selenomethionine 200 microg daily and/or celecoxib 200 mg twice daily (2 x 2 factorial design) among residents of Linxian, People's Republic of China. (nih.gov)
- Methods: We conducted a randomized, controlled trial of selenomethionine 200 μg daily and/or celecoxib 200 mg twice daily (2 × 2 factorial design) among residents of Linxian, People's Republic of China. (elsevierpure.com)
- Conclusions: After a 10-month intervention, neither selenomethionine nor celecoxib inhibited esophageal squamous carcinogenesis for all high-risk subjects. (elsevierpure.com)
Sodium selenate1
- It was selenomethionine, or sodium selenite or sodium selenate or mustard seed extract selenium? (earthclinic.com)
Esophageal squamous2
- In unplanned stratified analyses, selenomethionine favorably affected a change in dysplasia grade among 115 subjects with mild esophageal squamous dysplasia at baseline (P = .02), but not among 123 subjects with moderate esophageal squamous dysplasia at baseline (P = 1.00). (elsevierpure.com)
- However, among subjects with mild esophageal squamous dysplasia at baseline, selenomethionine did have a protective effect. (elsevierpure.com)
Selenocysteine2
- Most selenium in animal tissues is present as selenomethionine or selenocysteine. (cdc.gov)
- Selenomethionine can be supplemented to generate the organically complexed and active selenocysteine. (healthy.net)
Proteins3
- However, the incorporation of selenomethionine into tissue proteins and keratin in cattle, birds, and fish causes alkali disease. (wikipedia.org)
- The high-selenomethionine preparations of the proteins had no greater effect in quenching the peroxynitrite than did the normal-selenomethionine preparations. (nih.gov)
- These results do not support the proposal that selenomethionine in proteins contributes to in vivo protection against peroxynitrite. (nih.gov)
Protective effects1
- 14. The protective effects of DL-Selenomethionine against T-2/HT-2 toxins-induced cytotoxicity and oxidative stress in broiler hepatocytes. (nih.gov)
Organic1
- It has been suggested by nutritionists that selenomethionine, as an organic form of selenium, is easier for the human body to absorb than selenite, which is an inorganic form. (wikipedia.org)
Vivo1
- Selenomethionine has been suggested to protect against peroxynitrite by quenching it in vivo. (nih.gov)
Antioxidant5
- Selenomethionine (Se-Met), a major bioactive form of selenium (Se) in organisms with significant antioxidant capacity, reduced the levels of total tau and hyperphosphorylated tau and ameliorated cognitive deficits in younger triple transgenic AD (3xTg-AD) mice. (nih.gov)
- 11. Dietary selenomethionine increases antioxidant capacity of geese by improving glutathione and thioredoxin systems. (nih.gov)
- 12. Effects of different levels of dietary hydroxy-analogue of selenomethionine on growth performance, selenium deposition and antioxidant status of weaned piglets. (nih.gov)
- 13. Beneficial antioxidant status of piglets from sows fed selenomethionine compared with piglets from sows fed sodium selenite. (nih.gov)
- 15. Effects of hydroxy-selenomethionine on performance, innate immune system and antioxidant defense of tambaqui (Colossoma macropomum) exposed to a physical stressor. (nih.gov)
Butanoic1
- Please visit SDS Safety Data Sheet of 2-Amino-4-(methylselanyl)butanoic Acid or L-selenomethionine Suppliers . (ammol.org)
Dysplasia1
- Overall, selenomethionine resulted in a trend toward increased dysplasia regression (43% vs 32%) and decreased dysplasia progression (14% vs 19%) compared with no selenomethionine (P = .08). (nih.gov)
Thyroid function2
- Thorne Research Selenium (formerly Selenomethionine) is an essential mineral that supports heart health, thyroid function, and optimal immune function. (supplementfirst.com)
- Selenomethionine has been shown to be essential for proper thyroid function in particular conversion of T4 to T3 the active form of the thyroid hormone. (brain-bean.com)
Species2
- The L-selenomethionine enantiomer is the main form of selenium found in Brazil nuts, cereal grains, soybeans, and grassland legumes, while Se-methylselenocysteine, or its γ-glutamyl derivative, is the major form of selenium found in Astragalus, Allium, and Brassica species. (wikipedia.org)
- 17. Effects of sodium selenite and L-selenomethionine on feed intake, clinically relevant blood parameters and selenium species in plasma, colostrum and milk from high-yielding sows. (nih.gov)
Content2
- L-selenomethionine is produced by chemical synthesis which thecomposition is clear and content is accurate. (track4win.com)
- The customers can test the content ofL-selenomethionine themselves and easily do the quality control. (track4win.com)
Immune3
- Using L-selenomethionine in your diets will result in improved performance, immune function and higher economical return for your aquacultural production! (orffa.com)
- 9. Selenomethionine ameliorates LPS-induced intestinal immune dysfunction in chicken jejunum. (nih.gov)
- Phospholipase C, immune inhibitor A, chitin-binding protein and a single peptide match to chain A crystal structure of selenomethionine were observed in the secretions of L. infantum promastigotes. (who.int)
Effect6
- L-selenomethionine can effectively pass placenta and breast barriers toexpress strong maternal effect. (track4win.com)
- 1. Protective effect of selenomethionine on intestinal injury induced by T- 2 toxin. (nih.gov)
- 2. Protective effect of selenomethionine on T-2 toxin-induced liver injury in New Zealand rabbits. (nih.gov)
- 4. Protective Effect of Selenomethionine on T-2 Toxin-Induced Rabbit Immunotoxicity. (nih.gov)
- 19. Protective effect of selenomethionine on kidney injury induced by ochratoxin A in rabbits. (nih.gov)
- There was no effect after the same incubation period with concentrations of up to 0.03 millimoles of selenomethionine (1464422), but with concentrations as low as 0.0125 millimoles of sodium-selenite (10102188) there was significant toxicity to the cells. (cdc.gov)
Methods1
- L-selenomethionine can bequalitative quantitative tested by HPCL, which the method is mature , reliableand the result is accurate ( USP, EFSA and Ministry of Agriculture in China isusing the same or similar methods). (track4win.com)
Analysis1
- L-selenomethionine:Method of Analysis is mature and easy, which is easily for customers themselvesto do quality control. (track4win.com)