OrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation Science
MyoglobinWhalesMetmyoglobinMyoglobinuriaHemeHorsesCetaceaSperm WhaleCarbon MonoxideRhabdomyolysisPhotolysisSpectrophotometryCreatine KinaseHemeproteinsHemoglobinsSpectrum Analysis, RamanOxygenLeghemoglobinElephantsProtein ConformationHistidineBromotrichloromethaneSeals, EarlessSpectrum AnalysisCarboxyhemoglobinApoproteinsClinical Enzyme TestsLigandsKineticsSpectrophotometry, InfraredHeminElectron Spin Resonance SpectroscopyIronMagnetic Resonance SpectroscopyOxidation-ReductionAmino Acid SequenceMolecular Sequence Data
Myoglobin
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
Whales
Large marine mammals of the order CETACEA. In the past, they were commercially valued for whale oil, for their flesh as human food and in ANIMAL FEED and FERTILIZERS, and for baleen. Today, there is a moratorium on most commercial whaling, as all species are either listed as endangered or threatened.
Metmyoglobin
Myoglobin which is in the oxidized ferric or hemin form. The oxidation causes a change in color from red to brown.
Myoglobinuria
Heme
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
Horses
Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.
Cetacea
An order of wholly aquatic MAMMALS occurring in all the OCEANS and adjoining seas of the world, as well as in certain river systems. They feed generally on FISHES, cephalopods, and crustaceans. Most are gregarious and most have a relatively long period of parental care and maturation. Included are DOLPHINS; PORPOISES; and WHALES. (From Walker's Mammals of the World, 5th ed, pp969-70)
Sperm Whale
The species Physeter catodon (also called Physeter macrocephalus), in the family Physeteridae. The common name is derived from the milky wax substance in its head (spermaceti). The species also produces an intestinal secretion AMBERGRIS, which was previously used in perfumes. The sperm whale is the largest toothed MAMMAL in the world.
Carbon Monoxide
Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)
Rhabdomyolysis
Necrosis or disintegration of skeletal muscle often followed by myoglobinuria.
Photolysis
Chemical bond cleavage reactions resulting from absorption of radiant energy.
Spectrophotometry
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Creatine Kinase
A transferase that catalyzes formation of PHOSPHOCREATINE from ATP + CREATINE. The reaction stores ATP energy as phosphocreatine. Three cytoplasmic ISOENZYMES have been identified in human tissues: the MM type from SKELETAL MUSCLE, the MB type from myocardial tissue and the BB type from nervous tissue as well as a mitochondrial isoenzyme. Macro-creatine kinase refers to creatine kinase complexed with other serum proteins.
Hemeproteins
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
Hemoglobins
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.
Spectrum Analysis, Raman
Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.
Oxygen
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.
Leghemoglobin
A hemoglobin-like oxygen-binding hemeprotein present in the nitrogen-fixing root nodules of leguminous plants. The red pigment has a molecular weight approximately 1/4 that of hemoglobin and has been suggested to act as an oxido-reduction catalyst in symbiotic nitrogen fixation.
Elephants
Large mammals in the family Elephantidae, with columnar limbs, bulky bodies, and elongated snouts. They are the only surviving members of the PROBOSCIDEA MAMMALS.
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Histidine
An essential amino acid that is required for the production of HISTAMINE.
Bromotrichloromethane
A potent liver poison. In rats, bromotrichloromethane produces about three times the degree of liver microsomal lipid peroxidation as does carbon tetrachloride.
Seals, Earless
The family Phocidae, suborder PINNIPEDIA, order CARNIVORA, comprising the true seals. They lack external ears and are unable to use their hind flippers to walk. It includes over 18 species including the harp seal, probably the best known seal species in the world.
Spectrum Analysis
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Carboxyhemoglobin
Apoproteins
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
Clinical Enzyme Tests
Analyses for a specific enzyme activity, or of the level of a specific enzyme that is used to assess health and disease risk, for early detection of disease or disease prediction, diagnosis, and change in disease status.
Ligands
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
Kinetics
The rate dynamics in chemical or physical systems.
Spectrophotometry, Infrared
Spectrophotometry in the infrared region, usually for the purpose of chemical analysis through measurement of absorption spectra associated with rotational and vibrational energy levels of molecules. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Hemin
Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.
Electron Spin Resonance Spectroscopy
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
Iron
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
Magnetic Resonance Spectroscopy
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
Oxidation-Reduction
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Amino Acid Sequence
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

The determination of hemoglobin and myoglogin residues as a parameter for testing heat exposure in back bacon. (1/1729)

The use of an extraction of the heme pigments hemoglobin and myoglobin as a test for the heat exposure of back bacon was investigated by treating back bacon at varying temperatures of 50-70 degrees C and times of two to 180 minutes and observing the effect on the absorbance of heme pigment residue after nitrite oxidation. Absorbance at 409 nm was used in place of the more usual 540 nm to provide greater sensitivity in the detection of heme. A decrease in residual heme pigments was time-dependent, particularly at lower temperatures. In view of this factor and the complex nature of the heat exposure of a large block of back bacon, the application of this test would require a calibration of each process. Alternatively, limits to the amounts of heme pigment residue could be set. The heme pigment test is useful in its simplicity and overcomes difficulties associated with the coagulation and enzyme tests.  (+info)

Myocardial oxygenation during high work states in hearts with postinfarction remodeling. (2/1729)

BACKGROUND: Postinfarction left ventricular remodeling (LVR) is associated with reductions in myocardial high-energy phosphate (HEP) levels, which are more severe in animals that develop overt congestive heart failure (CHF). During high work states, further HEP loss occurs, which suggests demand-induced ischemia. This study tested the hypothesis that inadequate myocyte oxygen availability is the basis for these HEP abnormalities. METHODS AND RESULTS: Myocardial infarction was produced by left circumflex coronary artery ligation in swine. Studies were performed in 20 normal animals, 14 animals with compensated LVR, and 9 animals with CHF. Phosphocreatine (PCr)/ATP was determined with 31P NMR and deoxymyoglobin (Mb-delta) with 1H NMR in myocardium remote from the infarct. Basal PCr/ATP tended to be decreased in postinfarct hearts, and this was significant in animals with CHF. Infusion of dobutamine (20 microg x kg-1 x min-1 IV) caused doubling of the rate-pressure product in both normal and LVR hearts and resulted in comparable significant decreases of PCr/ATP in both groups. This decrease in PCr/ATP was not associated with detectable Mb-delta. In CHF hearts, rate-pressure product increased only 40% in response to dobutamine; this attenuated response also was not associated with detectable Mb-delta. CONCLUSIONS: Thus, the decrease of PCr/ATP during dobutamine infusion is not the result of insufficient myocardial oxygen availability. Furthermore, in CHF hearts, the low basal PCr/ATP and the attenuated response to dobutamine occurred in the absence of myocardial hypoxia, indicating that the HEP and contractile abnormalities were not the result of insufficient oxygen availability.  (+info)

Structural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10). (3/1729)

A triple mutant of sperm whale myoglobin (Mb) [Leu(B10) --> Tyr, His(E7) --> Gln, and Thr(E10) --> Arg, called Mb-YQR], investigated by stopped-flow, laser photolysis, crystallography, and molecular dynamics (MD) simulations, proved to be quite unusual. Rebinding of photodissociated NO, O2, and CO from within the protein (in a "geminate" mode) allows us to reach general conclusions about dynamics and cavities in proteins. The 3D structure of oxy Mb-YQR shows that bound O2 makes two H-bonds with Tyr(B10)29 and Gln(E7)64; on deoxygenation, these two residues move toward the space occupied by O2. The bimolecular rate constant for NO binding is the same as for wild-type, but those for CO and O2 binding are reduced 10-fold. While there is no geminate recombination with O2 and CO, geminate rebinding of NO displays an unusually large and very slow component, which is pretty much abolished in the presence of xenon. These results and MD simulations suggest that the ligand migrates in the protein matrix to a major "secondary site," located beneath Tyr(B10)29 and accessible via the motion of Ile(G8)107; this site is different from the "primary site" identified by others who investigated the photolyzed state of wild-type Mb by crystallography. Our hypothesis may rationalize the O2 binding properties of Mb-YQR, and more generally to propose a mechanism of control of ligand binding and dissociation in hemeproteins based on the dynamics of side chains that may (or may not) allow access to and direct temporary sequestration of the dissociated ligand in a docking site within the protein. This interpretation suggests that very fast (picosecond) fluctuations of amino acid side chains may play a crucial role in controlling O2 delivery to tissue at a rate compatible with physiology.  (+info)

Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate. (4/1729)

On exposure to mildly acidic conditions, apomyoglobin forms a partially folded intermediate, I. The A, B, G, and H helices are significantly structured in this equilibrium intermediate, whereas the remainder of the protein is largely unfolded. We report here the effects of mutations at helix pairing sites on the stability of I in three classes of mutants that: (i) truncate hydrophobic side chains in native helix packing sites, (ii) truncate hydrophobic side chains not involved in interhelical contacts, and (iii) extend hydrophobic side chains at residues not involved in interhelical contacts. Class I mutants significantly decrease the stability and cooperativity of folding of the intermediate. Class II and III mutants show smaller effects on stability and have little effect on cooperativity. Qualitatively similar results to those found in I were obtained for all three classes of mutants in native myoglobin (N), demonstrating that hydrophobic burial is fairly specific to native helix packing sites in I as well as in N. These results suggest that hydrophobic burial along native-like interhelical contacts is important for the formation of the cooperatively folded intermediate.  (+info)

Development of diving capacity in emperor penguins. (5/1729)

To compare the diving capacities of juvenile and adult emperor penguins Aptenodytes forsteri, and to determine the physiological variables underlying the diving ability of juveniles, we monitored diving activity in juvenile penguins fitted with satellite-linked time/depth recorders and examined developmental changes in body mass (Mb), hemoglobin concentration, myoglobin (Mb) content and muscle citrate synthase and lactate dehydrogenase activities. Diving depth, diving duration and time-at-depth histograms were obtained from two fledged juveniles during the first 2.5 months after their depature from the Cape Washingon colony in the Ross Sea, Antarctica. During this period, values of all three diving variables increased progressively. After 8-10 weeks at sea, 24-41 % of transmitted maximum diving depths were between 80 and 200 m. Although most dives lasted less than 2 min during the 2 month period, 8-25 % of transmitted dives in the last 2 weeks lasted 2-4 min. These values are lower than those previously recorded in adults during foraging trips. Of the physiological variables examined during chick and juvenile development, only Mb and Mb content did not approach adult values. In both near-fledge chicks and juveniles, Mb was 50-60 % of adult values and Mb content was 24-31 % of adult values. This suggests that the increase in diving capacity of juveniles at sea will be most dependent on changes in these factors.  (+info)

Low molecular weight heparin (dalteparin) as adjuvant treatment of thrombolysis in acute myocardial infarction--a pilot study: biochemical markers in acute coronary syndromes (BIOMACS II). (6/1729)

OBJECTIVES: This randomized, double blind, placebo-controlled pilot trial evaluated the effect of dalteparin as an adjuvant to thrombolysis in patients with acute myocardial infarction regarding early reperfusion, recurrent ischemia and patency at 24 h. BACKGROUND: Low-molecular-weight heparin, given subcutaneously twice daily without monitoring, might be an attractive alternative to conventional intravenous heparin in the treatment of acute myocardial infarction. METHODS: In 101 patients dalteparin/placebo 100 IU/kg was given just before streptokinase and a second injection 120 IU/kg after 12 h. Monitoring with continuous vector-ECG was done to obtain signs of early reperfusion and later ischemic episodes. Blood samples for myoglobin were obtained at start and after 90 min to evaluate signs of reperfusion. Coronary angiography was performed after 20-28 h to evaluate TIMI-flow in the infarct-related artery. RESULTS: Dalteparin added to streptokinase tended to provide a higher rate of TIMI grade 3 flow in infarct-related artery compared to placebo, 68% versus 51% (p = 0.10). Dalteparin had no effects on noninvasive signs of early reperfusion. In patients with signs of early reperfusion, there seemed to be a higher rate of TIMI grade 3 flow, 74% versus 46% (myoglobin) (p = 0.04) and 73% versus 52% (vector-ECG) (p = 0.11). Ischemic episodes 6-24 h. after start of treatment were fewer in the dalteparin group, 16% versus 38% (p = 0.04). CONCLUSIONS: When dalteparin was added as an adjuvant to streptokinase and aspirin, there were tendencies for less ECG monitoring evidence of recurrent ischemia and better patency at 24 h, warranting further study.  (+info)

Direct sedimentation analysis of interference optical data in analytical ultracentrifugation. (7/1729)

Sedimentation data acquired with the interference optical scanning system of the Optima XL-I analytical ultracentrifuge can exhibit time-invariant noise components, as well as small radial-invariant baseline offsets, both superimposed onto the radial fringe shift data resulting from the macromolecular solute distribution. A well-established method for the interpretation of such ultracentrifugation data is based on the analysis of time-differences of the measured fringe profiles, such as employed in the g(s*) method. We demonstrate how the technique of separation of linear and nonlinear parameters can be used in the modeling of interference data by unraveling the time-invariant and radial-invariant noise components. This allows the direct application of the recently developed approximate analytical and numerical solutions of the Lamm equation to the analysis of interference optical fringe profiles. The presented method is statistically advantageous since it does not require the differentiation of the data and the model functions. The method is demonstrated on experimental data and compared with the results of a g(s*) analysis. It is also demonstrated that the calculation of time-invariant noise components can be useful in the analysis of absorbance optical data. They can be extracted from data acquired during the approach to equilibrium, and can be used to increase the reliability of the results obtained from a sedimentation equilibrium analysis.  (+info)

Convective oxygen transport and tissue oxygen consumption in Weddell seals during aerobic dives. (8/1729)

Unlike their terrestrial counterparts, marine mammals stop breathing and reduce their convective oxygen transport while performing activities (e.g. foraging, courtship, aggressive interactions, predator avoidance and migration) that require sustained power output during submergence. Since most voluntary dives are believed to remain aerobic, the goal of this study was to examine the potential importance of the dive response in optimizing the use of blood and muscle oxygen stores during dives involving different levels of muscular exertion. To accomplish this, we designed a numerical model based on Fick's principle that integrated cardiac output (Vb), regional blood flow, convective oxygen transport (Q(O2)), muscle oxymyoglobin desaturation and regional rates of oxygen consumption (VO2). The model quantified how the optimal matching or mismatching of QO2 to VO2 affected the aerobic dive limit (ADL). We chose an adult Weddell seal Leptonycotes weddellii on which to base our model because of available data on the diving physiology and metabolism of this species. The results show that the use of blood and muscle oxygen stores must be completed at the same time to maximize the ADL for each level of VO2. This is achieved by adjusting Vb (range 19-94 % of resting levels) and muscle QO2 according to the rate of muscle oxygen consumption (VMO2). At higher values of VMO2, Vb and muscle perfusion must increase to maintain an appropriate QO2/VO2 ratio so that available blood and muscle oxygen stores are depleted at the same time. Although the dive response does not sequester blood oxygen exclusively for brain and heart metabolism during aerobic dives, as it does during forced submersion, a reduction in Vb and muscle perfusion below resting levels is necessary to maximize the ADL over the range of diving VO2 (approximately 2-9 ml O2 min-1 kg-1). Despite the reduction in Vb, convective oxygen transport is adequate to maintain aerobic metabolism and normal function in the splanchnic organs, kidneys and other peripheral tissues. As a result, physiological homeostasis is maintained throughout the dive. The model shows that the cardiovascular adjustments known as the dive response enable the diving seal to balance the conflicting metabolic demands of (1) optimizing the distribution and use of blood and muscle oxygen stores to maximize the ADL over the normal range of diving VO2 and (2) ensuring that active muscle receives adequate oxygen as VMO2 increases.  (+info)

Electron Transfer in Ruthenium/Zinc Porphyrin Derivatives of Recombinant Human Myoglobins. Analysis of Tunneling Pathways in...Electron Transfer in Ruthenium/Zinc Porphyrin Derivatives of Recombinant Human Myoglobins. Analysis of Tunneling Pathways in...
TY - JOUR. T1 - Electron Transfer in Ruthenium/Zinc Porphyrin Derivatives of Recombinant Human Myoglobins. Analysis of Tunneling Pathways in Myoglobin and Cytochrome c. AU - Casimiro, Danilo R.. AU - Wong, Luet L.. AU - Colón, Jorge L.. AU - Zewert, Thomas E.. AU - Richards, John H.. AU - Chang, I. Jy. AU - Winkler, Jay R.. AU - Gray, Harry B.. PY - 1993/2/1. Y1 - 1993/2/1. N2 - Site-directed mutants of human myoglobin have been prepared and characterized; each protein has a single surface-modifiable histidine (at position 48, 70, or 83). The proteins were modified by covalent attachment of pentaammineruthenium (a5Ru) to the surface histidine and substitution of zinc mesoporphyrin IX diacid (ZnP) for the heme. Donor-acceptor separations (edge-edge distances d) in the modified proteins are 9.5 Å, His70; 12.7 Å, His48; and 15.5 Å, His83. Rates of photoinduced electron transfer in these ruthenium-modified myoglobins were measured by transient absorption spectroscopy. The 3ZnP*→ Ru3+ rate ...
https://scholar.lib.ntnu.edu.tw/en/publications/electron-transfer-in-rutheniumzinc-porphyrin-derivatives-of-recom
Roles of Proximal Ligand in Heme Proteins: Replacement of Proximal Histidine of Human Myoglobin with Cysteine and Tyrosine by...Roles of Proximal Ligand in Heme Proteins: Replacement of Proximal Histidine of Human Myoglobin with Cysteine and Tyrosine by...
TY - JOUR. T1 - Roles of Proximal Ligand in Heme Proteins. T2 - Replacement of Proximal Histidine of Human Myoglobin with Cysteine and Tyrosine by Site-Directed Mutagenesis as Models for P-450, Chloroperoxidase, and Catalase. AU - Adachi, Shin Ichi. AU - Nagano, Shingo. AU - Ishimori, Koichiro. AU - Watanabe, Yoshihito. AU - Morishima, Isao. AU - Egawa, Tsuyoshi. AU - Kitagawa, Teizo. AU - Makino, Ryu. PY - 1993/1/1. Y1 - 1993/1/1. N2 - Histidine-93(F8) in human myoglobin (Mb), which is the proximal ligand of the heme iron, has been replaced with cysteine or tyrosine by site-directed mutagenesis. The resultant proximal cysteine and tyrosine mutant Mbs (H93C and H93Y Mbs, respectively) exhibit the altered axial ligation analogous to P-450, chloroperoxidase, and catalase. Coordination of cysteine or tyrosine to the ferric heme iron is confirmed by spectroscopic measurements including electronic absorption, hyperfine-shifted 1H-NMR, EPR, resonance Raman spectroscopies, and redox potential ...
https://einstein.pure.elsevier.com/en/publications/roles-of-proximal-ligand-in-heme-proteins-replacement-of-proximal-2
Gentaur Molecular :Kamiya \ Human Myoglobin ELISA \ KT-503Gentaur Molecular :Kamiya \ Human Myoglobin ELISA \ KT-503
Gentaur molecular products has all kinds of products like :search , Kamiya \ Human Myoglobin ELISA \ KT-503 for more molecular products just contact us
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CIRCULATING AUTOANTIBODY AGAINST HUMAN MYOGLOBIN IN POLYMYOSITIS.CIRCULATING AUTOANTIBODY AGAINST HUMAN MYOGLOBIN IN POLYMYOSITIS.
O:13:\PanistOpenUrl\:36:{s:10:\\u0000*\u0000openUrl\;N;s:6:\\u0000*\u0000idc\;N;s:6:\\u0000*\u0000fmt\;s:7:\journal\;s:6:\\u0000*\u0000doi\;s:0:\\;s:6:\\u0000*\u0000pii\;s:0:\\;s:7:\\u0000*\u0000pmid\;s:0:\\;s:9:\\u0000*\u0000atitle\;s:65:\CIRCULATING AUTOANTIBODY AGAINST HUMAN MYOGLOBIN IN POLYMYOSITIS.\;s:9:\\u0000*\u0000jtitle\;s:0:\\;s:9:\\u0000*\u0000stitle\;s:0:\\;s:7:\\u0000*\u0000date\;s:4:\1977\;s:9:\\u0000*\u0000volume\;s:0:\\;s:8:\\u0000*\u0000issue\;s:0:\\;s:8:\\u0000*\u0000spage\;s:0:\\;s:8:\\u0000*\u0000epage\;s:0:\\;s:8:\\u0000*\u0000pages\;s:0:\\;s:7:\\u0000*\u0000issn\;s:0:\\;s:8:\\u0000*\u0000eissn\;s:0:\\;s:9:\\u0000*\u0000aulast\;s:8:\NISHIKAI\;s:10:\\u0000*\u0000aufirst\;s:1:\M\;s:9:\\u0000*\u0000auinit\;N;s:10:\\u0000*\u0000auinitm\;N;s:5:\\u0000*\u0000au\;a:2:{i:0;s:10:\NISHIKAI M\;i:1;s:7:\HOMMA ...
https://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=PASCAL7750443533
Unscramble myoglobins | Words unscrambled from letters myoglobins | Scrabble Word myoglobins | Words Made with the Letters...Unscramble myoglobins | Words unscrambled from letters myoglobins | Scrabble Word myoglobins | Words Made with the Letters...
Unscramble myoglobins, Unscramble letters myoglobins, Point value for myoglobins, Word Decoder for myoglobins, Word generator using the letters myoglobins, Word Solver myoglobins, Possible Scrabble words with myoglobins, Anagram of myoglobins
http://www.allscrabblewords.com/word-description/myoglobins
Section 8 RG.docx - CHEMISTRY 445 - Myoglobin and Hemoglobin Watch the lecture videos on myoglobin and hemoglobin Answers to...Section 8 RG.docx - CHEMISTRY 445 - Myoglobin and Hemoglobin Watch the lecture videos on myoglobin and hemoglobin Answers to...
View Section_8_RG.docx from CHEM 445 at Sonoma State University. CHEMISTRY 445 - Myoglobin and Hemoglobin Watch the lecture videos on myoglobin and hemoglobin. Answers to some of the reading guide
https://www.coursehero.com/file/48974145/Section-8-RGdocx/
Recombinant Human Myoglobin Heme free T7 | Cell SciencesRecombinant Human Myoglobin Heme free T7 | Cell Sciences
Prices are in US dollars.. These products are for laboratory research purposes only, not for any human or animal diagnostic or therapeutic use.. All site content © 2019 Cell Sciences, Inc.. ...
https://www.cellsciences.com/recombinant-human-myoglobin-heme-free-t7-1
Native Human Myoglobin | Bio-Rad Antibodies (formerly AbD Serotec)Native Human Myoglobin | Bio-Rad Antibodies (formerly AbD Serotec)
Bio-Rad Antibodies (formerly AbD Serotec) is the research antibody division of Bio-Rad, the worlds leading life science company.
https://www.bio-rad-antibodies.com/human-myoglobin-purified-protein-6450-1104.html
Iron in the structure of Nitromethane Modified Horse Heart Myoglobin (pdb 2nsr)
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Iron atom in PDB 2nsr: Nitromethane Modified Horse Heart Myoglobin
http://iron.atomistry.com/pdb2nsr.html
A harántcsíkolt izom rosttípusainak jellemzése sarcoplasmaticus reticulum (SR) Ca2+-ATP-áz és myoglobin immunhisztokémiával.<...
TY - JOUR. T1 - A harántcsíkolt izom rosttípusainak jellemzése sarcoplasmaticus reticulum (SR) Ca2+-ATP-áz és myoglobin immunhisztokémiával.. AU - Krenács, T.. AU - Molnár, E.. AU - Dobó, E.. AU - Dux, L.. PY - 1989/4/1. Y1 - 1989/4/1. N2 - By the immunohistochemical demonstration of SR calcium ATPase and myoglobin a fibre classification method was developed. Fast fibres showed intense, while slow fibres weak SR calcium ATPase reactivity. Immunohistochemical reaction of myoglobin characterized the oxidative metabolic state of fibres similar to the succinate dehydrogenase (SDH) reaction. By means of SR calcium ATPase and myoglobin immunohistochemistry fibres were classified as slow oxidative (SO), fast oxidative glycolytic (FOG) and fast glycolytic (Fg) groups. The SR calcium ATPase activity of the different fibres varied in the FG greater than FOG greater than SO order, while myoglobin immunoreactivity in the FOG greater than SO greater than FG order. Both proteins studied preserved ...
https://hungary.pure.elsevier.com/en/publications/characterization-of-striated-muscle-fiber-types-by-ca2-atpase-and
Identification and modeling of protein conformational substatesIdentification and modeling of protein conformational substates
The range of conformations of macromolecules and the dynamic interconversion between conformations is an important part of the relationship between structure and function. The existence of side-chain conformational substates in two systems is directly demonstrated using traditional X-ray crystallographic refinement methodologies. One system is a mutant met-myoglobin where the phenylalanine at position 46 was replaced by a valine. The other is a low-temperature high-resolution dataset for wild-type CO myoglobin, Multi-conformer refinements, which combine molecular dynamics with X-ray data restraints, are shown to model side-chain substates similar to those identified manually. The two conformations of his64 in the mutant myoglobin and wild-type myoglobin, and three conformations of ser117 in the wild-type myoglobin are found automatically. Time averaged refinements, which also use a modified molecular dynamics algorithm but is a simulation rather than strictly an optimization, also found ...
https://scholarship.rice.edu/handle/1911/19423
Assignment of heme and distal amino-acid resonances in the h-1-NMR spectra of the carbon-monoxide and oxygen complexes of sperm...Assignment of heme and distal amino-acid resonances in the h-1-NMR spectra of the carbon-monoxide and oxygen complexes of sperm...
Assignments of resonances of the heme and distal amino acid protons in spectra of the CO and O2 complexes of sperm whale myoglobin are reported. These resonances provide information on the conformation of the heme pocket. For oxymyoglobin, the assignments of the heme meso protons disagree with those proposed previously on the basis of partial deuteration experiments. Rapid ring flips about the C beta-C gamma bond are detected for Phe-CD1. Recent claims for two conformational substates of valine-E11 in carbonmonoxymyoglobin (Bradbury, J.H. and Carver, J.A. (1984) Biochemistry 23, 4905-4913) are shown to be in error. The pK of His-97 (FG3) in carbonmonoxymyoglobin has been determined (pK = 5.9). This residue appears to influence many spectroscopic properties of myoglobin. The distal His-E7 in carbonmonoxymyoglobin has pK less than 5.0. Differences in the heme pocket conformation in the CO complexes of myoglobin and leghemoglobin are discussed. These differences may be influential in O2 and CO ...
https://vivo.scripps.edu/display/endnote271333
Myoglobin - DocCheck FlexikonMyoglobin - DocCheck Flexikon
Myoglobin is a globular protein and consists of eight α-helixes in its secondary structure. Myoglobin is a protein composed of a single polypeptide chain build by 153 amino acids. The polypeptide chain is bound to a heme molecule which represents the prosthetic group of myoglobin. The heme is bound to a histidine residue at position 93 (His93 or His-F8) within the N-terminal end of the myoglobin polypeptide. If oxygen is bound to heme, the distal histidine at position 64 (called His64 or His-E7) contributes to the stabilization of the oxygen which binds to iron (Fe2+) within the heme structure. ...
https://flexikon.doccheck.com/en/Myoglobin
Myoglobin - Simple English Wikipedia, the free encyclopediaMyoglobin - Simple English Wikipedia, the free encyclopedia
Myoglobin is a protein that is able to bind oxygen. Myoglobin, which is similar to haemoglobin, is the main oxygen-carrying pigment of muscle tissues.[1] Like haemoglobin, it has a porphyrin ring with an iron atom at its centre. It is in the muscle tissue of most mammals. Seals and other marine mammals have more myoglobin in their muscles than land animals. In humans, increased level of myoglobin in the serum of the blood can be an indication of myocardial infarction. Other factors for a higher level can be damage to the muscles, epileptic seizures, polytrauma. If the value is much too high, this can lead to kidney failure. ...
https://simple.wikipedia.org/wiki/Myoglobin
Myoglobin (human) AlphaLISA Detection Kit, 5,000 Assay Points | PerkinElmerMyoglobin (human) AlphaLISA Detection Kit, 5,000 Assay Points | PerkinElmer
AlphaLISA no-wash assay kit for detection and quantitation of Human Myoglobin in serum, buffered solution or cell culture medium.
https://www.perkinelmer.com/product/alphalisa-myoglobin-kit-5-000-assay-pts-al285f
1998 - Creatine kinase-MB, cardiac troponin T, and myoglobin levels identified failed reperfusion after thrombolysis...1998 - Creatine kinase-MB, cardiac troponin T, and myoglobin levels identified failed reperfusion after thrombolysis...
The results of the study by Stewart and colleagues confirm previous findings showing that successful coronary reperfusion leads to an accelerated increase in the levels of plasma markers of myocardial injury in patients treated with thrombolytic therapy for MI (1-3). Changes in the level of myoglobin have been found in almost all previous studies to be useful in detecting coronary reperfusion but may lack specificity because this marker is not cardiac-specific. Rapid increases in CKMB, MB isoforms, and troponin may offer enhanced specificity but may be less sensitive because early changes in levels of these compounds are less marked than those of myoglobin. Differences also exist in the performance of the available assays for these markers. This is important for development of clinical criteria for failure of reperfusion. Nonetheless, available data suggest that using ratios of 60- and 90-minute levels to the initial levels of some of these markers is reasonably accurate for assessing the ...
http://www.acpjc.org/Content/129/3/issue/ACPJC-1998-129-3-071.htm
Effects of formylation of vinyl side chains of heme on optical and ligand binding properties of horse heart ferric myoglobin |...
Effects of substitution of vinyl groups of hemin with formyl groups on the optical and ligand binding properties of horse heart ferric myoglobin were investigated. The peak positions as well as the line shapes of the absorption spectra of the ferric derivatives of three kinds of formylmyoglobin, 2-vinyl-4-formyl-, 2-formyl-4-vinyl-, and 2,4-diformylmyoglobins depend on the number and the position of the formyl groups. Absorption maxima in the Soret region of the acid forms of these ferric formylmyoglobins in 0.1 M potassium phosphate buffer, pH 6.0, at 20 degrees were 415.2, 422, and 429 nm, respectively. The acid forms of these formylmyoglobins exhibit absorption spectra of the mixture of high- and low spin states at ambient temperature. Since proto-, deutero- and mesomyoglobins have a high spin state under the same condition, the increase of the low spin iron in these formylmyoglobins may be due to the strong electron withdrawal by the formyl groups toward the periphery of the porphyrin ring. ...
https://www.meta.org/papers/effects-of-formylation-of-vinyl-side-chains-of/4456
What is Myoglobin? What is the function of Myoglobin?What is Myoglobin? What is the function of Myoglobin?
What is Myoglobin? What is the function of Myoglobin? This is the basic structure and functions of Myoglobin. This short notes includes the major points now
https://biochemden.com/myoglobin/
Structural determinants of functional behavior in distal pocket mutants of myoglobinStructural determinants of functional behavior in distal pocket mutants of myoglobin
The physiological role of myoglobin depends on the modulation of heme activity by the protein. The hypothesis that functional properties are governed by conserved residues in the distal pocket has been tested by site-directed mutagenesis of three residues: Leu$\sp{29}$, His$\sp{64}$, and Val$\sp{68}$. To facilitate interpretation of functional data, structures of several mutant myoglobins have been determined by X-ray crystallography. Leu$\sp{29}$ controls the volume of the distal pocket. Since Val$\sp{29}$ does not contact bound ligands, this substitution does not affect ligand affinities significantly. It does permit solvent approach to the heme, thereby increasing the rate of autooxidation. Although the Phe$\sp{29}$ mutant was constructed to reduce the volume of the binding site, dipole-multipole interactions stabilize bound oxygen and reduce the rate of autooxidation substantially. His$\sp{64}$ inhibits oxygen dissociation and autooxidation by hydrogen bonding to the ligand. In conjunction ...
https://scholarship.rice.edu/handle/1911/16871?show=full
Collective motions and structural self-organisation along the myoglobin folding pathwayCollective motions and structural self-organisation along the myoglobin folding pathway
We develop a highly predictive energy function to describe the low temperature crystallographic structure of myoglobin with sub-\AA ngstr\om precision. We use the energy function to investigate the way how myoglobin folds.For this we employ the Glauber protocol, with a variable ambient temperature. We first increase the temperature so that the structure unfolds into a random coil. We then lower thetemperature back to its original value, and monitor how the myoglobin folds towards its native state.We find that the folding proceeds by $\alpha$-helix nucleation, and that the ordering of helix formation parallels experimental observations. There is also a molten globule folding intermediate, with a radius of gyration that matches the experimentally measured value. We estimate the relative folding times between a random chain and molten globule, and between molten globule and the native state, and we find that the ratio is consistentwith the experimentally measured values. We also propose a number ...
http://uu.diva-portal.org/smash/record.jsf?pid=diva2:748721
Structure and Function of Hemoglobin and Myoglobin - ChemistryScoreStructure and Function of Hemoglobin and Myoglobin - ChemistryScore
Hemoglobin (HbA) and fetal hemoglobin (HbF) resemble a sigmoidal curve when it comes to oxygen binding affinity.. This is because hemoglobin has something called cooperative interaction between binding sites.. Cooperative binding = binding of a ligand to one site increases affinity for a ligand at another binding site.. Since hemoglobin is a tetramer, cooperative binding plays an important role.. The p50 (pressure required for hemoglobin to be 50% bound to oxygen) is much higher as opposed to myoglobin.. This allows for the blood to deliver more oxygen to the tissues than myoglobin since the binding affinity is less than that of myoglobin.. Hemoglobin binding to oxygen can be defined using the Hill Equation:. ...
https://chemistryscore.com/hemoglobin-and-myoglobin-function/
Mini-myoglobin: native-like folding of the NO-derivative. | Pubblicazioni Scientifiche UnicamMini-myoglobin: native-like folding of the NO-derivative. | Pubblicazioni Scientifiche Unicam
Mini-myoglobin is a polypeptide fragment (residues 32-139) obtained by limited proteolysis of horse heart apomyoglobin and reconstituted with the natural heme. Its functional properties are very similar to those of native myoglobin and therefore it may represent a model for testing the functional role of the protein fragment encoded by the central exon of myoglobin gene (residues 31-105). Here we have investigated some properties of the nitric oxide derivative of mini-myoglobin in comparison with those of NO-myoglobin, to provide more structural information on the heme pocket residues in addition to that already acquired by electron paramagnetic resonance of the cobalt-substituted mini-myoglobin. At pH 7.0, optical and circular dichroism Soret spectra, as well as electron paramagnetic resonance spectra reveal that the heme orientation in the pocket and the coordination state of the ferrous iron in NO-mini-myoglobin are similar to those of the whole protein. The spectra of the NO-mini-myoglobin ...
https://pubblicazioni.unicam.it/handle/11581/243084
Structural Biochemistry/Protein function/Myoglobins Oxygen Binding Curve - Wikibooks, open books for an open worldStructural Biochemistry/Protein function/Myoglobins Oxygen Binding Curve - Wikibooks, open books for an open world
Myoglobin has a strong affinity for oxygen when it is in the lungs, and where the pressure is around 100 torr. When it reaches the tissues, where its around 20 torr, the affinity for oxygen is still quite high. This makes myoglobin less efficient of an oxygen transporter than hemoglobin, which loses its affinity for oxygen as the pressure goes down and releases the oxygen into the tissues. Myoglobins strong affinity for oxygen means that it keeps the oxygen binded to itself instead of releasing it into the tissues. ...
https://en.wikibooks.org/wiki/Structural_Biochemistry/Protein_function/Myoglobin%27s_Oxygen_Binding_Curve
Catalysts | Free Full-Text | Oxygen Storage Capacity and Oxygen Mobility of Co-Mn-Mg-Al Mixed Oxides and Their Relation in ...Catalysts | Free Full-Text | Oxygen Storage Capacity and Oxygen Mobility of Co-Mn-Mg-Al Mixed Oxides and Their Relation in ...
Co-Mn-Mg-Al oxides were synthesized using auto-combustion and co-precipitation techniques. Constant ratios were maintained with (Co + Mn + Mg)/Al equal to 3.0, (Co + Mn)/Mg equal to 1.0 and Co/Mn equal to 0.5. The chemical and structural composition, redox properties, oxygen storage capacity and oxygen mobility were analyzed using X-ray fluorescence (XRF), X-ray diffraction (XRD), Raman spectroscopy, scanning electron microscopy (SEM), temperature-programmed reduction of hydrogen (H2-TPR), oxygen storage capacity (OSC), oxygen storage complete capacity (OSCC) and isotopic exchange, respectively. The catalytic behavior of the oxides was evaluated in the total oxidation of a mixture of 250 ppm toluene and 250 ppm 2-propanol. The synthesis methodology affected the crystallite size, redox properties, OSC and oxide oxygen mobility, which determined the catalytic behavior. The co-precipitation method got the most active oxide in the oxidation of the volatile organic compound (VOC) mixture because of the
http://www.mdpi.com/2073-4344/5/2/905
Insulation Paper for Liquid Oxygen StorageInsulation Paper for Liquid Oxygen Storage
Buy Insulation Paper for Liquid Oxygen Storage, Find Details include Size,Weight,Model and Width about Insulation Paper for Liquid Oxygen Storage. Make an Inquiry for Insulation Paper for Liquid Oxygen Storage at OKorder.com.
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Myoglobin molecule - Stock Image F006/9417 - Science Photo LibraryMyoglobin molecule - Stock Image F006/9417 - Science Photo Library
Myoglobin, molecular model. Myoglobin is a protein found in muscle tissue, where it binds to and stores oxygen to be used during strenuous exercise. The structure of the globin protein protects the haem (iron) group from being oxidised and destroyed by the oxygen it carries. - Stock Image F006/9417
http://www.sciencephoto.com/media/525691/view
Myoglobin molecule - Stock Image F009/6153 - Science Photo LibraryMyoglobin molecule - Stock Image F009/6153 - Science Photo Library
Myoglobin, molecular model. Myoglobin is a protein found in muscle tissue, where it binds to and stores oxygen to be used during strenuous exercise. The structure of the globin protein protects the haem (iron) group from being oxidised and destroyed by the oxygen it carries. - Stock Image F009/6153
http://www.sciencephoto.com/media/597335/view
The effects of aging temperature and aging time on the oxygen storage capacity of Pt-Rh/CeZrO2 catalystsThe effects of aging temperature and aging time on the oxygen storage capacity of Pt-Rh/CeZrO2 catalysts
HORI, C.E. et al. The effects of aging temperature and aging time on the oxygen storage capacity of Pt-Rh/CeZrO2 catalysts. Braz. J. Chem. Eng. [online]. 2001, vol.18, n.1, pp.23-33. ISSN 0104-6632. http://dx.doi.org/10.1590/S0104-66322001000100003.. The effects of aging temperature and time on the oxygen storage capacity (OSC) of Pt-Rh-promoted Ce0.75Zr0.25O2 solid solutions were measured and correlated with the BET surface area and noble metal (NM) surface area in the catalysts. The NM surface area is better correlated with OSC than is with the BET surface area. On a practical level, our results demonstrated that, even when operating at 900°C with alternating oxidizing and reducing conditions, these materials deactivate slowly with a near t-1 time dependence. Deactivation rates for these catalysts are dependent on the NM loading with the highest loaded catalysts deactivating roughly half as fast as the lowest loaded catalysts. As the aging temperature is increased from 900°C to 1000°C, the ...
http://www.scielo.br/scielo.php?script=sci_abstract&pid=S0104-66322001000100003&lng=pt&nrm=iso&tlng=en
Myoglobin, Serum - Mayo Clinic Laboratories | Cardiology Catalog
1. Lamb EJ, Jones GRD: Kidney functions tests. In: Rifai N, Horvath AR, Wittwer CT, eds. Tietz Textbook of Clinical Chemistry and Molecular Diagnostics. 6th ed. Elsevier; 2018:489. 2. Cappenllini MD, Lo SF, Swinkels DW. Hemoglobin, iron, bilirubin. In: Rifai N, Horvath AR, Wittwer CT, eds. Tietz Textbook of Clinical Chemistry and Molecular Diagnostics. 6th ed. Elsevier; 2018:747. 3. Varki AP, Roby DS, Watts H, Zatuchni J: Serum myoglobin in acute myocardial infarction: a clinical study and review of the literature. Am Heart J. 1978;96:680-688. 4. Kallner A, Sylven C, Brodin U, et al: Early diagnosis of acute myocardial infarction. A comparison between chemical predictors. Scand J Clin Lab Invest. 1989;49:633-639. ...
https://cardiology.testcatalog.org/show/MYGLS
Rapid myoglobin aggregation through... | ERARapid myoglobin aggregation through... | ERA
The extent of glycation and conformational changes of horse myoglobin (Mb) upon glycation with N-acetyl-glucosamine (GlcNAc), glucose...
https://era.library.ualberta.ca/items/86c27fd1-f581-440e-930c-27cd7ff1c81d
Is there a relation between myocardial salvage and the release patterns of myoglobin and creatine kinase-MB in acute myocardial...Is there a relation between myocardial salvage and the release patterns of myoglobin and creatine kinase-MB in acute myocardial...
Is there a relation between myocardial salvage and the release patterns of myoglobin and creatine kinase-MB in acute myocardial infarction submitted to thrombolysic ...
http://orbi.ulg.ac.be/handle/2268/67774
Oxygen mystery: How marine mammals hold their breath - Xenophilia
The team extracted pure myoglobin from the muscles of mammals - from the land-based cow, to the semi-aquatic otter, all the way up elite divers like the sperm whale.. Led by researcher Scott Mirceta, this painstaking examination traced the changes in myoglobin in deep-diving mammals through 200 million years of evolutionary history.. And it revealed that the best breath-holding divers in the mammal family had evolved a non-stick variety of myoglobin.. The secret, Dr Berenbrink explained, was a subtle but crucial piece of chemical trickery; marine mammal myoglobin is positively charged.. This has important physical consequences. Dr Berenbrink explained: Like the similar poles of a magnet; the proteins repel one another.. In this way we think the animals are able to pack really high concentrations of these proteins into their muscles and avoid them sticking together and clogging up the muscles.. Dr Berenbrink said he was excited by the discovery because it helped make sense of the incredible ...
https://xenophilia.com/oxygen-mystery-how-marine-mammals-hold-their-breath/
Exhausted on Dauphin Steet?Exhausted on Dauphin Steet?
Binding to myoglobin, potentially causing myocardial and skeletal muscle dysfunction.. The most clear-cut mechanism by which CO toxicity occurs is competitive binding to the hemoglobin heme groups. ...The net result is a hemoglobin molecule that is poorly equipped to release oxygen at the tissue level. The decreased oxygen delivery is then sensed centrally, stimulating ventilatory efforts and increasing minute ventilation.... The mean half-life of COHb is 320 minutes (128- 409) in young healthy volunteers on room air. Administration of one hundred percent O2 at one atmosphere reduces the half life to 80.3 minutes, while 100% O2 at three atmospheres will reduce the half life to 23.3 minutes. CO binds to cardiac and skeletal myoglobin as well as hemoglobin (Hb). Cardiac myoglobin binds three times more CO than skeletal myoglobin..... By now, if youre still reading, you may be wondering just what the heck this all means. Well, in a nutshell, it means that if you like training along Dauphin Street ...
http://www.racewalking.org/exhauste.htm
Proton NMR study of the mechanism of the heme-apoprotein reaction for myoglobin<...
TY - JOUR. T1 - Proton NMR study of the mechanism of the heme-apoprotein reaction for myoglobin. AU - Jue, Thomas. AU - Krishnamoorthi, R.. AU - La Mar, Gerd N.. PY - 1983. Y1 - 1983. UR - http://www.scopus.com/inward/record.url?scp=0000836440&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0000836440&partnerID=8YFLogxK. M3 - Article. AN - SCOPUS:0000836440. VL - 105. SP - 5701. EP - 5703. JO - Journal of the American Chemical Society. JF - Journal of the American Chemical Society. SN - 0002-7863. IS - 17. ER - ...
https://ucdavis.pure.elsevier.com/en/publications/proton-nmr-study-of-the-mechanism-of-the-heme-apoprotein-reaction
RELAXATIONS AND FLUCTUATIONS IN MYOGLOBIN (Conference) | SciTech ConnectRELAXATIONS AND FLUCTUATIONS IN MYOGLOBIN (Conference) | SciTech Connect
One major goal of biological physics is the discovery and understanding of the concepts and laws that govern biomolecules, in particular proteins. Since there exist at least 10{sup 5} different proteins, the choice of a suitable prototype is necessary. Myoglobin (Mb) has for many years played the role of such a prototype. It appears to be simple enough so that many of its properties can be understood, yet it is complex enough to display many of the fascinating characteristics of biomolecules. One major achievement in the study of any protein would be the establishment of convincing connections among structure, kinetics, energy landscape, dynamics, and function. We believe that this goal has not yet been reached in any protein, but the present knowledge of Mb gives some hope that the end is near in this case. Here we sketch some of the results that have been obtained in the past fifty or more years in the research on Mb, obtained by an army of investigators. ...
https://www.osti.gov/scitech/biblio/768895-relaxations-fluctuations-myoglobin
hemoglobin and myoglobin - CHEMISTRY COMMUNITYhemoglobin and myoglobin - CHEMISTRY COMMUNITY
what is the difference in the chemical structures of hemoglobin and myoglobin? Both consist of the same heme complex and a binded protein correct ...
https://lavelle.chem.ucla.edu/forum/viewtopic.php?p=200875
hemoglobin and myoglobin - CHEMISTRY COMMUNITYhemoglobin and myoglobin - CHEMISTRY COMMUNITY
what is the difference in the chemical structures of hemoglobin and myoglobin? Both consist of the same heme complex and a binded protein correct ...
https://lavelle.chem.ucla.edu/forum/viewtopic.php?t=54423
Significance of the amino acid composition of proteins I Composition of hemoglobins and myoglobins in relation to their...Significance of the amino acid composition of proteins I Composition of hemoglobins and myoglobins in relation to their...
Atassi, M. Z., 1966: Significance of the amino acid composition of proteins I Composition of hemoglobins and myoglobins in relation to their structure, function and evolution
https://eurekamag.com/research/025/454/025454230.php
Hemoglobin & Myoglobin Lesson | Pre Nursing Course | NURSING.comHemoglobin & Myoglobin Lesson | Pre Nursing Course | NURSING.com
Check out this lesson on the hemoglobin & myoglobin & learn everything you will need to know on for Pre-Nursing. View the lesson today!
https://nursing.com/lesson/01-01-hemoglobin-and-myoglobin/
Hemoglobin Notes - Myoglobin, TheamountofoxygenHemoglobin Notes - Myoglobin, Theamountofoxygen
View Notes - Hemoglobin Notes from CH 369 at University of Texas. Myoglobin,anoxygenbindingprotein Hasapolypeptidechainwithanironcontaininghemegroup.
https://www.coursehero.com/file/5909385/Hemoglobin-Notes/
Genetic control of the immune response to myoglobin. V. Antibody prod by Y Kohno and J A. BerzofskyGenetic control of the immune response to myoglobin. V. Antibody prod by Y Kohno and J A. Berzofsky
Kohno, Y and Berzofsky, J A., Genetic control of the immune response to myoglobin. V. Antibody production in vitro is macropahge and t cell-dependent and is under control of two determinant-specific ir genes. (1982). Subject Strain Bibliography 1982. 2543 ...
https://mouseion.jax.org/ssbb1982/2543/
Gentaur Molecular :Assaypro \ Cardiac Myoglobin, anti human IgG \ 11461-05015Gentaur Molecular :Assaypro \ Cardiac Myoglobin, anti human IgG \ 11461-05015
Gentaur molecular products has all kinds of products like :search , Assaypro \ Cardiac Myoglobin, anti_human IgG \ 11461-05015 for more molecular products just contact us
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Myoglobin | Naked Science ForumMyoglobin | Naked Science Forum
I was wondering today whether it would be possible to isolate myoglobin from the blood of a deep diving sea mammal, and cultivate it to inject into humans - ...
https://www.thenakedscientists.com/forum/index.php?topic=7841.0
Myoglobin, Serum : Purpose & Normal Range of Results | 1mgMyoglobin, Serum : Purpose & Normal Range of Results | 1mg
Myoglobin, Serum : View interpretation of results, purpose, procedure, answers to patient concerns/FAQs and book at lowest prices from labs and diagnostic centers in your city on 1mg.com.
https://www.1mg.com/labs/test/myoglobin-serum-1521
Myoglobin Antibodies | Bio-RadMyoglobin Antibodies | Bio-Rad
We have brought together our full range of myoglobin products in one place, making it easier for you to find exactly what you need.
https://www.bio-rad-antibodies.com/myoglobin-antibody-range.html
人Myoglobin ELISA试剂盒 | Abcam中国官方网站人Myoglobin ELISA试剂盒 | Abcam中国官方网站
人Myoglobin ELISA试剂盒ELISA试剂盒datasheet (ab108652).Abcam抗体、ELISA、激动剂拮抗剂、表观遗传试剂、蛋白多肽，使用效果保证，中国70%以上现货。
http://www.abcam.cn/human-myoglobin-elisa-kit-ab108652.html
X-ray spectroscopy reveals iron spin state in oxygenated hemoproteinsX-ray spectroscopy reveals iron spin state in oxygenated hemoproteins
Aerobic life on earth requires efficient management of molecular oxygen (O2). Nature has developed proteins that bind an iron-porphyrin (heme) cofactor as versatile O2 managers. Such hemoproteins, in particular in animals and humans, have been extensively studied, for example, establishing cooperative versus non-cooperative O2 binding to heme iron in tetrameric hemoglobin and monomeric myoglobin, respectively. Today, rising interest in this topic stems from the ongoing discovery of globins with broad functionality in plants and microorganisms.. Three physiologically-relevant heme species can be distinguished in myoglobin and hemoglobin: the ligand-free (deoxy), carbon-monoxide inhibited (carboxy), and O2-bound (oxy) forms. Paramagnetic behaviour has established high-spin Fe(II) in deoxy whereas carboxy is diamagnetic due to low-spin Fe(II). For oxy, a diamagnetic cofactor has been proven. A controversy has remained on the nature of the iron-oxygen bonding in myoglobin and hemoglobin, dating back ...
http://www.esrf.eu/fr/home/news/spotlight/content-news/spotlight/spotlight301.html
In the face of hypoxia : myoglobin expression under hypoxic conditions in cultured Weddell seal skeletal muscle cellsIn the face of hypoxia : myoglobin expression under hypoxic conditions in cultured Weddell seal skeletal muscle cells
The hallmark adaptation to breath-hold diving in Weddell seals (Leptonychotes weddellii) is enhanced concentrations of myoglobin in their skeletal muscles. Myoglobin is a cytoplasmic hemoprotein that stores oxygen for use in aerobic metabolism throughout the dive duration. In addition, throughout the duration of the dive, Weddell seals rely on oxygen stored in myoglobin to sustain aerobic metabolism in which lipid is the primary contributor of acetyl CoA for the citric acid cycle. Together, enhanced myoglobin concentrations and a lipid-based aerobic metabolism represent some of the unique ...
https://dspace.library.colostate.edu/handle/10217/65322
Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis | Biochemical JournalFunctional and structural characterization of the myoglobin from the polychaete Ophelia bicornis | Biochemical Journal
The myoglobin of the polychaete annelid Ophelia bicornis was isolated, purified to homogeneity and characterized. The primary structure, obtained from cDNA and protein sequencing, consists of 139 amino acid residues. The alignment with other globin sequences showed that O. bicornis myoglobin misses the pre-A helix and the first six residues of the A helix. The presence of a PheB10-GlnE7 haem distal residue pair is in agreement with the measured oxygen affinity (P50=0.85 mmHg; 1 mmHg=0.133 kPa) and the only slightly higher autoxidation rate constant (0.28 h−1) with respect to that of the sperm whale myoglobin mutant E7 His→Gln (0.21 h−1) and to elephant myoglobin (0.1 h−1). Oxygen-binding co-operativity was found to be absent under all the examined experimental conditions. The resistance of O. bicornis myoglobin towards autoxidation seems to confirm the important role of part of the A helix in the stability of the globin. The higher pKa of the acid-alkaline ferric transition of O. ...
http://www.biochemj.org/content/389/2/497
Myoglobin - WikipediaMyoglobin - Wikipedia
Myoglobin is the primary oxygen-carrying pigment of muscle tissues.[7] High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin.[6] Myoglobin is found in Type I muscle, Type II A and Type II B, but most texts consider myoglobin not to be found in smooth muscle. Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystallography.[8] This achievement was reported in 1958 by John Kendrew and associates.[9] For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz.[10] Despite being one of the most studied proteins in biology, its physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin can be viable and fertile but show many cellular and physiological adaptations to overcome the loss. Through observing these changes in ...
https://en.m.wikipedia.org/wiki/Myoglobin
Iron in the structure of Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser on [300 Min] (pdb 2zsn)
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Iron atom in PDB 2zsn: Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser on [300 Min]
http://iron.atomistry.com/pdb2zsn.html
Serum concentrations of myoglobin vs human heart-type cytoplasmic fatty acid-binding protein in early detection of acute...Serum concentrations of myoglobin vs human heart-type cytoplasmic fatty acid-binding protein in early detection of acute...
TY - JOUR. T1 - Serum concentrations of myoglobin vs human heart-type cytoplasmic fatty acid-binding protein in early detection of acute myocardial infarction. AU - Ishii, J.. AU - Wang, J.. AU - Naruse, H.. AU - Taga, S.. AU - Kinoshita, M.. AU - Kurokawa, H.. AU - Iwase, M.. AU - Kondo, T.. AU - Nomura, M.. AU - Nagamura, Y.. AU - Watanabe, Y.. AU - Hishida, H.. AU - Tanaka, T.. AU - Kawamura, K.. PY - 1997/8/19. Y1 - 1997/8/19. N2 - We compared the diagnostic utility of serum concentrations of human heart-type cytoplasmic fatty acid-binding protein (H-FABPc), myoglobin, and their ratio for the early diagnosis of acute myocardial infarction (AMI) in 104 healthy volunteers and 165 patients at admission within 6 h of the onset of chest pain. The ROC curves of the H-FABPc [0.946, 95% confidence interval (CI) = 0.913-0.979] and myoglobin (0.895, 95% CI = 0.8460.944) between patients with AMI and healthy volunteers were significantly greater than the area under the ratio of myoglobin to H-FABPc ...
https://pure.fujita-hu.ac.jp/en/publications/serum-concentrations-of-myoglobin-vs-human-heart-type-cytoplasmic
Identification Through DNA Analysis in Criminal and Family-Relatedness Investigations<...Identification Through DNA Analysis in Criminal and Family-Relatedness Investigations<...
TY - CHAP. T1 - Identification Through DNA Analysis in Criminal and Family-Relatedness Investigations. AU - Allen, Robert W.. N1 - Copyright: Copyright 2013 Elsevier B.V., All rights reserved.. PY - 2010. Y1 - 2010. N2 - This chapter discusses the identification through DNA analysis in criminal and family-relatedness investigations. Genetic polymorphisms in chromosomal DNA revolutionized the field of identification testing and radically improved the level of certainty in conclusions issued by labs performing parentage or forensic testing. The variability in DNA discovered were associated with the human myoglobin gene. DNA fingerprints could be visualized in human genomic DNA using the then-rather-standard molecular technique known as restriction fragment length polymorphism analysis. The highly variable DNA markers visualized through RFLP analysis group exhibited a molecular structure consisting of a short sequence of nucleotides that was tandemly repeated a variable number of times along a ...
https://scholars.okstate.edu/en/publications/identification-through-dna-analysis-in-criminal-and-family-relate
Concentrations of myoglobin and myoglobin mRNA in heart ventricles from Antarctic fishes | Journal of Experimental BiologyConcentrations of myoglobin and myoglobin mRNA in heart ventricles from Antarctic fishes | Journal of Experimental Biology
We used a combined immunochemical and molecular approach to ascertain the presence and concentrations of both the intracellular oxygen-binding hemoprotein myoglobin (Mb) and its messenger RNA (mRNA) in 13 of 15 known species of Antarctic channichthyid icefishes. Mb protein is present in the hearts of eight species of icefishes: Chionodraco rastrospinosus, Chionodraco hamatus, Chionodraco myersi, Chaenodraco wilsoni, Pseudochaenichthys georgianus, Cryodraco antarcticus, Chionobathyscus dewitti and Neopagetopsis ionah. Five icefish species lack detectable Mb protein: Chaenocephalus aceratus, Pagetopsis macropterus, Pagetopsis maculatus, Champsocephalus gunnari and Dacodraco hunteri. Mb concentrations range from 0.44+/−0.02 to 0.71+/−0.08 mg Mb g(−)(1)wet mass in heart ventricle of species expressing the protein. A Mb-mRNA-specific cDNA probe was used to quantify mRNA in five Mb-expressing icefishes. Mb mRNA was found in low but detectable amounts in Champsocephalus gunnari, one of the ...
https://jeb.biologists.org/content/203/8/1277?ijkey=55323afdf26e3136c27870f7152e493bc1e755a2&keytype2=tf_ipsecsha
Concentrations of myoglobin and myoglobin mRNA in heart ventricles from Antarctic fishes | Journal of Experimental BiologyConcentrations of myoglobin and myoglobin mRNA in heart ventricles from Antarctic fishes | Journal of Experimental Biology
We used a combined immunochemical and molecular approach to ascertain the presence and concentrations of both the intracellular oxygen-binding hemoprotein myoglobin (Mb) and its messenger RNA (mRNA) in 13 of 15 known species of Antarctic channichthyid icefishes. Mb protein is present in the hearts of eight species of icefishes: Chionodraco rastrospinosus, Chionodraco hamatus, Chionodraco myersi, Chaenodraco wilsoni, Pseudochaenichthys georgianus, Cryodraco antarcticus, Chionobathyscus dewitti and Neopagetopsis ionah. Five icefish species lack detectable Mb protein: Chaenocephalus aceratus, Pagetopsis macropterus, Pagetopsis maculatus, Champsocephalus gunnari and Dacodraco hunteri. Mb concentrations range from 0.44+/−0.02 to 0.71+/−0.08 mg Mb g(−)(1)wet mass in heart ventricle of species expressing the protein. A Mb-mRNA-specific cDNA probe was used to quantify mRNA in five Mb-expressing icefishes. Mb mRNA was found in low but detectable amounts in Champsocephalus gunnari, one of the ...
http://jeb.biologists.org/content/203/8/1277
CellNetworks - Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation
The hemoprotein myoglobin is a model system for the study of protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond. Structural changes appear throughout the protein within 500 femtoseconds, with the C, F, and H helices moving away from the heme cofactor and the E and A helices moving toward it. These collective movements are predicted by hybrid quantum mechanics/molecular mechanics simulations. Together with the observed oscillations of residues contacting the heme, our calculations support the prediction that an immediate collective response of the protein occurs upon ligand dissociation, as a result of heme vibrational modes coupling to global modes of the protein ...
http://cellnetworks.uni-hd.de/936174/Direct_observation_of_ultrafast_collective_motions_in_CO_myoglobin_upon_ligand_dissociation
RCSB PDB - 1EMY: CRYSTAL STRUCTURE OF ASIAN ELEPHANT (ELEPHAS MAXIMUS) CYANO-MET MYOGLOBIN AT 1.78 ANGSTROMS RESOLUTION. PHE 29...RCSB PDB - 1EMY: CRYSTAL STRUCTURE OF ASIAN ELEPHANT (ELEPHAS MAXIMUS) CYANO-MET MYOGLOBIN AT 1.78 ANGSTROMS RESOLUTION. PHE 29...
1EMY: CRYSTAL STRUCTURE OF ASIAN ELEPHANT (ELEPHAS MAXIMUS) CYANO-MET MYOGLOBIN AT 1.78 ANGSTROMS RESOLUTION. PHE 29 (B10) ACCOUNTS FOR ITS UNUSUAL LIGAND BINDING PROPERTIES
https://www.rcsb.org/structure/1EMY
Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopy (Journal Article) | DOE PAGESObserving heme doming in myoglobin with femtosecond X-ray absorption spectroscopy (Journal Article) | DOE PAGES
We report time-resolved X-ray absorption measurements after photolysis of carbonmonoxy myoglobin performed at the LCLS X-ray free electron laser with nearly 100 fs (FWHM) time resolution. Data at the Fe K-edge reveal that the photoinduced structural changes at the heme occur in two steps, with a faster (~70 fs) relaxation preceding a slower (~400 fs) one. We tentatively attribute the first relaxation to a structural rearrangement induced by photolysis involving essentially only the heme chromophore and the second relaxation to a residual Fe motion out of the heme plane that is coupled to the displacement of myoglobin F-helix. ...
https://www.osti.gov/pages/biblio/1190858-observing-heme-doming-myoglobin-femtosecond-ray-absorption-spectroscopy
Strong iron demand during hypoxia-induced erythropoiesis is associated with down-regulation of iron-related proteins and...Strong iron demand during hypoxia-induced erythropoiesis is associated with down-regulation of iron-related proteins and...
Iron is essential for oxygen transport because it is incorporated in the heme of the oxygen-binding proteins hemoglobin and myoglobin. An interaction between iron homeostasis and oxygen regulation is further suggested during hypoxia, in which hemoglobin and myoglobin syntheses have been reported to increase. This study gives new insights into the changes in iron content and iron-oxygen interactions during enhanced erythropoiesis by simultaneously analyzing blood and muscle samples in humans exposed to 7 to 9 days of high altitude hypoxia (HA). HA up-regulates iron acquisition by erythroid cells, mobilizes body iron, and increases hemoglobin concentration. However, contrary to our hypothesis that muscle iron proteins and myoglobin would also be up-regulated during HA, this study shows that HA lowers myoglobin expression by 35% and down-regulates iron-related proteins in skeletal muscle, as evidenced by decreases in L-ferritin (43%), transferrin receptor (TfR; 50%), and total iron content (37%). ...
https://air.unimi.it/handle/2434/31817
Diving reflex - WikipediaDiving reflex - Wikipedia
Diving mammals have an elastic aortic bulb thought to help maintain arterial pressure during the extended intervals between heartbeats during dives, and have high blood volume, combined with large storage capacity in veins and retes of the thorax and head in seals and dolphins.[3] Chronic physiological adaptations of blood include elevated hematocrit, hemoglobin, and myoglobin levels which enable greater oxygen storage and delivery to essential organs during a dive.[3] Oxygen use is minimised during the diving reflex by energy efficient swimming or gliding behaviour, and regulation of metabolism, heart rate, and peripheral vasoconstriction.[3] Aerobic diving capacity is limited by available oxygen and the rate at which it is consumed. Diving mammals and birds have a considerably greater blood volume than terrestrial animals of similar size, and in addition have a far greater concentration of haemoglobin and myoglobin, and this haemoglobin and myoglobin is also capable of carrying a higher oxygen ...
https://en.wikipedia.org/wiki/Diving_reflex
Diving reflex - WikipediaDiving reflex - Wikipedia
Diving mammals have an elastic aortic bulb thought to help maintain arterial pressure during the extended intervals between heartbeats during dives, and have high blood volume, combined with large storage capacity in veins and retes of the thorax and head in seals and dolphins.[3] Chronic physiological adaptations of blood include elevated hematocrit, hemoglobin, and myoglobin levels which enable greater oxygen storage and delivery to essential organs during a dive.[3] Oxygen use is minimised during the diving reflex by energy efficient swimming or gliding behaviour, and regulation of metabolism, heart rate, and peripheral vasoconstriction.[3]. Aerobic diving capacity is limited by available oxygen and the rate at which it is consumed. Diving mammals and birds have a considerably greater blood volume than terrestrial animals of similar size, and in addition have a far greater concentration of haemoglobin and myoglobin, and this haemoglobin and myoglobin is also capable of carrying a higher ...
https://en.m.wikipedia.org/wiki/Diving_reflex
Mechanistic investigations of the reactions of peroxynitrite with hemoglobin and myoglobin - Research CollectionMechanistic investigations of the reactions of peroxynitrite with hemoglobin and myoglobin - Research Collection
ANORGANISCHE PEROXIDE + ANORGANISCHE PEROXOVERBINDUNGEN; SALPETRIGE SÄURE UND NITRITE (ANORGANISCHE CHEMIE); HÄMOGLOBIN (PROTEINE); MYOGLOBIN (PROTEINE, PEPTIDE); INORGANIC PEROXIDES + INORGANIC PEROXO-COMPOUNDS; NITROUS ACID AND NITRITES (INORGANIC CHEMISTRY); HEMOGLOBIN (PROTEINS); MYOGLOBIN (PROTEINS AND PEPTIDES ...
https://www.research-collection.ethz.ch/handle/20.500.11850/148119
Hemolytic Plaque Inhibition by Synthetic Antigenic Peptides of Sperm W by Elizabeth Moree Allen, Peter Abramoff et al.Hemolytic Plaque Inhibition by Synthetic Antigenic Peptides of Sperm W by Elizabeth Moree Allen, Peter Abramoff et al.
We have investigated the systemic antibody response to sperm whale myoglobin (SWMb) antigenic sites in three strains of inbred mice using an inhibition of plaque assay. Sperm whale myoglobin was attached to sheep red blood cells (SRBC) via rabbit anti-SRBC Fab fragments. Inhibition of lysis was obtained with synthetic peptides representing the purported five antigenic sites but not with a peptide whose sequence was unrelated to SWMb and synthetic peptides of SWMb from outside the antigenic sites gave minimal or no inhibition. The results of our studies show that the pattern of response to the five antigenic sites differs in each strain, but that almost total inhibition is obtained in all strains with these five sites. The antigenic dominance of these sites supports the concept of discrete antigenic sites on soluble proteins. They also suggest a reason for contrary reports in the literature based on hybridoma technology.
https://epublications.marquette.edu/bio_fac/337/
Exertional Rhabdomyolysis - What is it? - FasterSkier.com
After several years of training hard and working towards skiing fast, I am now in nurse practitioner school in - gulp - Connecticut. After reading Aubrey Smiths interview with Holly Brooks - fantastic piece by the way, and good luck Holly!!! - I wanted to learn more about rhabdomyolysis and exertional rhabdomyolysis. I decided I might as well share it with FasterSkier readers in case others had a similar curiosity to my own.. What is Rhabdo?. Rhabdomyolysis is the breakdown of skeletal muscle tissue resulting in the release of myoglobin into the blood stream, and from there, into the urine. (Like hemoglobin, myoglobin carries oxygen, but only in the muscle tissue.) The kidneys are responsible for removing the myoglobin from the blood, but myoglobin is toxic to the lining of the kidneys. So we have a bit of a catch-22… pushing too much myoglobin through the kidneys can result in renal failure. Furthermore, because dehydration often exacerbates rhabdomyolysis, thick blood and low blood volume ...
https://fasterskier.com/2009/12/exertional-rhabdomyolysis-what-is-it/
Low Frequency Resonance Raman Study of Myoglobin Derivatives by Helen S. BronderLow Frequency Resonance Raman Study of Myoglobin Derivatives by Helen S. Bronder
Bronder, Helen S., Low Frequency Resonance Raman Study of Myoglobin Derivatives (1992). Masters Theses (1922-2009) Access restricted to Marquette Campus. 2441 ...
http://epublications.marquette.edu/theses/2441/
DNA cleavage by oxymyoglobin and cysteine-introduced metmyoglobinDNA cleavage by oxymyoglobin and cysteine-introduced metmyoglobin
Double stranded DNA was cleaved oxidatively by incubation with oxygenated myoglobin, and Lys96Cys sperm whale myoglobin in its stable ferric form functioned as an artificial nuclease under air by formation of an oxygenated species, owing to electron transfer from the SH group of the introduced cysteine to the heme ...
https://library.naist.jp/dspace/handle/10061/10414
Hematopoietic stem/progenitor cells express myoglobin and neuroglobin: Adaptation to hypoxia or prevention from oxidative...Hematopoietic stem/progenitor cells express myoglobin and neuroglobin: Adaptation to hypoxia or prevention from oxidative...
Oxidative metabolism and redox signaling prove to play a decisional role in controlling adult hematopoietic stem/progenitor cells (HSPCs) biology. However, HSPCs reside in a hypoxic bone marrow microenvironment raising the question of how oxygen metabolism might be ensued. In this study, we provide for the first time novel functional and molecular evidences that human HSPCs express myoglobin (Mb) at level comparable with that of a muscle-derived cell line. Optical spectroscopy and oxymetry enabled to estimate an O-2-sensitive heme-containing protein content of approximately 180 ng globin per 10(6) HSPC and a P-50 of approximately 3 mu M O-2. Noticeably, expression of Mb mainly occurs through a HIF-1-induced alternative transcript (Mb-V/Mb-N = 35 +/- 15, p , .01). A search for other Mb-related globins unveiled significant expression of neuroglobin (Ngb) but not of cytoglobin. Confocal microscopy immune detection of Mb in HSPCs strikingly revealed nuclear localization in cell subsets expressing ...
https://ricerca.unich.it/handle/11564/676538
Rhabdomyolysis - Hotshot FitnessRhabdomyolysis - Hotshot Fitness
Takeaway: Rhabdo is not limited to one specific group of firefighters (all are at risk). Additionally, geography matters little. The cases were spread across the west about as evenly as possible.. What the heck Is Rhabdo?. Rhabdo occurs when skeletal muscle tissues are degraded to the point of disintegration, and begin to leech into your bloodstream. As your damaged muscle tissues breakdown, one of the by-products is a protein called myoglobin. As youll no doubt remember from your high school biology class, the kidney is working 24/7 to filter your blood. All the gunk it filters out is turned into urine. Which is why you pee. In a twenty-hour period, the average kidneys will filter around 120-150 quarts of blood and produce one to two quarts of urine. Well, as your muscle tissue is breaking down, and these myoglobins are entering your blood stream, you have a problem. Myoglobin is like Kryptonite to a kidney. The protein can cause some serious damage to the kidney, often times irreversible ...
https://www.hotshotfitness.com/rhabdomyolysis/
Understanding Meats: Why Red Meat is Red and Why White Meat is White - Crawford Farm Meats
Animal muscle turns to meat after slaughtering. Meat is surrounded by a layer of connective tissues, consisting almost entirely protein collagen. Meat tissues are composed of three main factors, water, protein (connective tissue) and fat. Carbohydrate also appears in meat as it gives the browning effect of meat when cooked. Without this carbohydrate, the desirable flavor and appearance of browned meat would not be achieved. Meat are mainly referred as red or dark and white meat. Red or dark meat is mainly made up of muscles with fibers that are called slow fibers. These muscles are used for extended periods of activity, such as standing or walking and need a consistent energy source. The protein myoglobin stores oxygen in muscle cells, which use oxygen to extract the energy needed for constant activity. Myoglobin is a richly pigmented protein. The more myoglobin there is in the cells, the redder or darker, the meat is. Red meat is red because the muscle fibers that make up the bulk of the meat ...
http://crawfordfarmmeatsetc.com/cooking-quality-meats/understanding-meats-why-red-meat-is-red-and-why-white-meat-is-white
Fujirebio Europe launches the Lumipulse® G hs Troponin I and Lumipulse G Myoglobin immunoassays for both the LUMIPULSE G1200...Fujirebio Europe launches the Lumipulse® G hs Troponin I and Lumipulse G Myoglobin immunoassays for both the LUMIPULSE G1200...
Fujirebio Europe has announced the release of the Lumipulse G hs Troponin I assay for use in the diagnosis of Acute Myocardial Infarction (AMI). In addition, the company also launches its Lumipulse G Myoglobin assay, both assays providing precise and sensitive results in 35 minutes.
https://www.fujirebio.com/en/news-events/fujirebio-europe-launches-the-lumipulser-g-hs-troponin-i-and-lumipulse-g-myoglobin
Limiting dilution comparison of the repertoires of high and low responder MHC-restricted T cells. | JEMLimiting dilution comparison of the repertoires of high and low responder MHC-restricted T cells. | JEM
To approach the mechanism that determines Ir gene-controlled high or low responsiveness to whole proteins, such as sperm whale myoglobin (SWMb), we compared the repertoires of high and low responder haplotype-restricted T cells for different myoglobin epitopes by limiting dilution frequency analysis. Poisson analysis was performed using long-term limiting dilution cell lines of (B10.BR [low] X B10.D2[high])F1 T cells maintained on high or low responder APCs. The cell lines were tested with SWMb peptides and fragments for T cell repertoire fine specificities and Ia restrictions. The frequency of SWMb-specific F1 T cells responsive on B10.BR (H-2k) APCs was 2.5-3.6-fold lower than on B10.D2 (H-2d) APCs. Strikingly, all of the H-2k-restricted T cells used I-Ek as a restriction element, whereas both I-Ad- and I-Ed-restricted T cells were found among the H-2d-restricted lines. The I-Ad-restricted T cells were dominant, and the majority was specific for the synthetic peptide 102-118. T cells specific ...
http://jem.rupress.org/content/167/3/1100
The colour of meat - Revision Cards in A Level and IB Revision SkillsThe colour of meat - Revision Cards in A Level and IB Revision Skills
Myoglobin and haemoglobin from the blood causes the red colour in meat. There is more myoglobin in well used muscle and in older animals this means the meat is darker. When oxygen is taken to the tissues the myoglobin is converted into oxymyoglobin, which is red. After slaughter the meat remains dark until it is cut and exposed to oxygen in the air when it becomes bright red. If stored for a long time the meat may become green or brown due to the effect of enzymes and bacteria. When meat is cooked the proteins denature making the meat firmer. The collagen is converted into gelatine in the presence of moisture. Elastin is softened slightly. Fat melts and penetrates the lean meat, increasing the energy value. The colour changes from red to brown. ...
https://getrevising.co.uk/revision-cards/the_colour_of_meat
Plate Tectonics And Continental Drift. - Pilots For 9/11 Truth ForumPlate Tectonics And Continental Drift. - Pilots For 9/11 Truth Forum
NOTE: Related to Hemoglobin is Myoglobin. Myoglobin forms pigments responsible for making meat red. The color that meat takes is partly determined by the oxidation states of the Iron atom in myoglobin and the oxygen species attached to it. When meat is in its raw state, the iron atom is in the +2 oxidation state, and is bound to a dioxygen molecule (O2). Meat cooked well done is brown because the iron atom is now in the +3 oxidation state, having lost an electron, and is now coordinated by a water molecule ...
http://pilotsfor911truth.org/forum/index.php?showtopic=12145&st=280&p=10796585
Acute Coronary Syndrome (ACS) - Clinical Pain AdvisorAcute Coronary Syndrome (ACS) - Clinical Pain Advisor
Troponins and CK-MB begin to appear in the circulation 3-4 hours after onset of injury, and levels reach maximal sensitivity for detection of necrosis by 6 hours. Levels may be too low to provide useful information when patients present within 6 hours of onset of symptoms, and clinicians should consider adding myoglobin when patients present within 6 hours of onset of symptoms. Myoglobin is released earlier (rises within 1 hour) than troponins and may afford earlier detection of myocardial injury. However, the utility of myoglobin is decreasing as the analytical sensitivity of troponin assays improves. Given the low to non-detectable circulating levels of troponins or CK-MB in the first few hours after onset, serial sampling is required to observe rises (or falls) of levels. CK-MB has poor specificity because of its presence in myocardial and skeletal muscle, as well as within the intestine, diaphragm, uterus, and prostate. Use of CK-MB in patients presenting with injury to these organs is ...
https://www.clinicalpainadvisor.com/home/decision-support-in-medicine/labmed/acute-coronary-syndrome-acs/
Neuroglobin, a novel member of the globin family, is expressed in focal regions of the brain<...
TY - JOUR. T1 - Neuroglobin, a novel member of the globin family, is expressed in focal regions of the brain. AU - Mammen, Pradeep P A. AU - Shelton, John M.. AU - Goetsch, Sean C.. AU - Williams, S. Clay. AU - Richardson, James A.. AU - Garry, Mary G.. AU - Garry, Daniel J.. PY - 2002/12/1. Y1 - 2002/12/1. N2 - Hemoproteins are widely distributed among unicellular eukaryotes, plants, and animals. In addition to myoglobin and hemoglobin, a third hemoprotein, neuroglobin, has recently been isolated from vertebrate brain. Although the functional role of this novel member of the globin family remains unclear, neuroglobin contains a heme-binding domain and may participate in diverse processes such as oxygen transport, oxygen storage, nitric oxide detoxification, or modulation of terminal oxidase activity. In this study we utilized in situ hybridization (ISH) and RT-PCR analyses to examine the expression of neuroglobin in the normoxic and hypoxic murine brain. In the normoxic adult mouse, neuroglobin ...
https://utsouthwestern.pure.elsevier.com/en/publications/neuroglobin-a-novel-member-of-the-globin-family-is-expressed-in-f
Influence du caractere culard sur la production et la qualité de la viande des bovins Blanc Bleu Belge - Clinquart AntoineInfluence du caractere culard sur la production et la qualité de la viande des bovins Blanc Bleu Belge - Clinquart Antoine
en] When compared to animals of the dual purpose type in the same breed, Belgian Blue double muscled bulls exhibit, at least, similar average daily gain with lower feed intake. The higher feed efficiency in the double muscled type is mainly explained by the composition of the weight gains, the muscle content is minimum 60 kg higher and the fat content 30 kg lower than in the dual purpose type when slaughtered at a similar liveweight. In both types, the dressing percentage and the lean meat proportion in the carcass increase with final liveweight.The chemical composition and the sensory characteristics of meat are also influenced by double muscling. The fat content is reduced and the polyunsaturated fatty acids proportion is increased in the double muscled type, resulting in a nutritional advantage. The difference in sensory characteristics could be, only partially, explained by the faster post mortem pH drop. The paler meat is mainly related to the myoglobin content. The advantage of the double ...
http://orbi.ulg.ac.be/handle/2268/61349
Iron out your body - Wellbeing India
Here comes the oxygen delivery service of your body!! The mineral iron makes the part heme of the famous hemoglobin. Hemoglobin is the substance of your red blood cell, which supplies oxygen to each and every cell of your body. Without oxygen any cell can not perform its function. For our muscles , myoglobin is the one who ensures adequate supply of oxygen to them. Here comes iron again!! Iron is also a part of this myoglobin. So too little iron meaning too little oxygen, lead to irritability, weakness, headaches, in severe cases , iron deficiency anemia.. ...
http://wellbeingindia.net/2012/11/08/iron-out-your-body/
RCPA - Myoglobin urineRCPA - Myoglobin urine
The RCPA is the leading organisation representing Pathologists and Senior Scientists in Australasia.. Its mission is to train and support pathologists and senior scientists and to improve the use of pathology testing to achieve better healthcare.. ...
https://www.rcpa.edu.au/Manuals/RCPA-Manual/Pathology-Tests/M/Myoglobin-urine
Plus itPlus it
The prototype low-pressure oxygen storage system performed well in both accelerated fatigue testing and in continuous (nonclinical) operation in a typical African health facility. Despite power interruptions, the flow of oxygen to a simulated patient was maintained without interruption for 30 d. Accelerated fatigue testing equivalent to , 2 y of operation yielded minimal signs of wear and tear. During power outages, the system operates automatically with no need either for another source of electricity or for user intervention. Preliminary testing indicates that the multilayer bladder system is rugged, long-lasting, and low-cost and offers the possibility of easy servicing by local technicians.. The low-pressure oxygen storage approach thus seems able to resolve some of the key problems restricting the use of oxygen concentrators in low-resource settings. The 200-L prototype would provide ,200 min of supply at a demand of 1 L/min, ,67 min at 3 L/min, or ,40 min at 5 L/min. (The storage pressure ...
http://rc.rcjournal.com/content/62/12/1582
Theoretical Model for the Study of CO Binding to Hemoproteins | SpringerLinkTheoretical Model for the Study of CO Binding to Hemoproteins | SpringerLink
We have analyzed the non-exponential kinetics, the temperature variation, and the CO isotope effects of the CO recombination reactions with myoglobin and single-chain hemoglobin.
https://link.springer.com/chapter/10.1007/978-3-642-85060-8_61
12:18 pm12:18 pm
Iron is necessary for many functions in the body including formation of hemoglobin, brain development and function regulation of body temperature, muscle activity and catecholamine metabolism. It is important for our immune system also. Lack of it directly affects the immune system; it diminished the number of T-cells and the production of antibodies. Beside hemoglobin, iron is component of myoglobin, the cytochromes, catalse and certain other enzyme systems. Iron is essential for binding oxygen to the blood cells. The central function of iron is oxygen transport and cell respiration.. ...
http://www.dailyhealthmagazine.com/iron/
Bachelors degree in Physiotherapy (to qualify as a physiotherapist) (Verona) | UniVr
2. Protein structure and function: aminoacid classification, buffering power, peptide bond, levels of protein structure; fibrous and globular proteins; hemoglobin and myoglobin: structure, function, factors influencing the oxygen bond; hemoglobin variants; enzymes: classification, role in the chemical reactions, regulation of the enzymatic activity ...
https://www.medicina.univr.it/main?ent=oi&aa=2017%2F2018&cs=477&discr=&discrCd=&id=112851&lang=en
Browsing Cattlemens Day, 2000 by Author Stroda, Sally L.Browsing Cattlemens Day, 2000 by Author Stroda, Sally L.
Beef quadriceps muscles from nine pH groups (5.5 - 6.4 in .1 increments) were ground; mixed with fat (20%); formed into patties whose myoglobin was in either the oxy or deoxy state; and cooked to four endpoint temperatures ...
http://krex.k-state.edu/dspace/handle/2097/4382/browse?value=Stroda%2C+Sally+L.&type=author
Harperın Resimli Biyokimyası - Biyoküre
Kitabın Orijinal Adı: Harpers Illustrated Biochemistry 28e. Editör(ler)/Yazar(lar): R.K. Murray ve ark.. Basım Yılı: 2009. Kitap İçeriği:. BÖLÜM 1: Biyokimya ve Tıp. (Biochemistry & Medicine). BÖLÜM 2: Su ve pH. (Water & pH). BÖLÜM 3: Amino Asitler ve Peptitler. (Amino Acids & Peptides). BÖLÜM 4: Proteinler: Birincil Yapısının Belirlenmesi. (Proteins: Determination of Primary Structure). BÖLÜM 5: Proteinler: Diğer Yüksek Yapılar. (Proteins: Higher Orders of Structure). BÖLÜM 6: Proteinler: Miyoglobin ve Hemoglobin. (Proteins: Myoglobin & Hemoglobin). BÖLÜM 7: Enzimler: Etki Mekanizması. (Enzymes: Mechanism of Action). BÖLÜM 8: Enzimler: Kinetik. (Enzymes: Kinetics). BÖLÜM 9: Enzimler: Aktivitelerinin Düzenlenmesi. (Enzymes: Regulation of Activities). BÖLÜM 10: Biyoinformatik ve Hesaplamalı Biyoloji. (Bioinformatics & Computational Biology). BÖLÜM 11: Biyoenerji: ATPnin Görevi. (Bioenergetics: The Role of ATP). BÖLÜM 12: Biyolojik ...
http://biyokure.org/2011/09/27/harperin-resimli-biyokimyasi/
Tests für CRP, D-Dimer und viele andere Parameter | ichromαTests für CRP, D-Dimer und viele andere Parameter | ichromα
ichroma testet in Ihrer Praxis: CRP, PCT, D-Dimer, Tn-I, CK-MB, Myoglobin, hsCRP, PSA, AFP, CEA, iFOB, HbA1c, Microalbumin, Cystantin C, TSH, TSH WB, TSH Plus, T3, T4, FSH, Progesterone, hCG, βhCG, LH, Prolactin, Testosterone, Cortisol, RF IgM, Ferritin, ASO
https://www.ichroma.at/en/tests/
The Nervous System - Revision Cards in A Level and IB BiologyThe Nervous System - Revision Cards in A Level and IB Biology
Slow twitch- contract slowly, used for keeping posture (e.g. back muscles) & endurance activities (e.g. posture, marathons). Long time without getting tired (energy released slowly- anaerobic). Many mitochondria, rich in myoglobin- store alot of O2.. Fast twitch- contract quickly, used for fast movement e.g. sprinting, blinking. release energy aerobically in short bursts, tire quickly. Few mitochondria, not much myoglobin (so cant store much O2).. ...
https://getrevising.co.uk/revision-cards/the_nervous_system_13
PhD Member | University of PittsburghPhD Member | University of Pittsburgh
How does the endogenous signaling molecule nitrite interact with the oxygen carrier myoglobin to regulate mitochondrial function and mediate cardioprotection? FIVE KEYWORDS THAT DESCRIBE YOUR AREAS OF INTEREST ...
http://www.dept-med.pitt.edu/PhD%20Community/Members/Shiva.html
Penbbs Vacuum FillerPenbbs Vacuum Filler
Industrial Vacuum Chopping Machine Cutting in vacuum environment It prevents the raw meat of myoglobin fat and other nutrients to be oxidized damage and reduces the bubbles existing The vacuum system is benefit for keeping the fresh color and taste of meat in maximum degree The high speed cutting system make it ...
https://www.processings.nl/dp-penbbs-vacuum-filler.html
Perpustakaan Digital ITB - WELCOME | Powered by GDL4.2
Kalibrasi kolom sephadex G-50 SF dilakukan dengan menggunakan campuran standar protein thyroglobulin (670 kDa), γ-globulin (158 kDa), ovalbumin (44 kDa), myoglobin (17 kDa), dan Vitamin B12 (1,35 kDa). Spesi yang terdeteksi setelah pemisahan dengan kolom sephadex G-50 SF dan kolom sephadex G-25 M berturut-turut diberi notasi subscript A dan subscript B. Subscript A1, A2, dan seterusnya menyatakan urutan spesi dari logam yang sama berdasarkan urutan berat molekul relatifnya. Metode QPNC PAGE diaplikasikan juga dalam penelitian ini untuk melihat profil elusi spesi unsur berdasarkan berbedaan m/z spesi. Kondisi operasional yang diterapkan meliputi (i) sistem buffer kontinyu 20 mM Tris-HCl/1 mM NaN3 pH 10, (ii) derajat polimerisasi poliakrilamid 4 %T / 2,67 % C, panjang gel 40 mm, fasa gerak 20 mM MES/1 mM NaN3 pH 8,0, dan (iii) temperatur analisis 4 derajat C. Sampel difraksinasi sebanyak 74 fraksi dengan volume setiap fraksi 5 mL (fraksinasi otomatis dengan pemograman). Pemisahan tahap dua spesi ...
http://digilib.itb.ac.id/gdl.php?mod=browse&op=read&id=jbptitbpp-gdl-noorfitrin-30966&q=Elemen
Near rhymes with rubinB-Rhymes | B-RhymesNear rhymes with rubinB-Rhymes | B-Rhymes
Near rhymes (words that almost rhyme) with rubin: blueprint, highfalutin, newsprint, myoglobin... Find more near rhymes/false rhymes at B-Rhymes.com
http://www.b-rhymes.com/rhyme/word/rubin
The Calcium Paradox: Its History and What It Really MeansThe Calcium Paradox: Its History and What It Really Means
Lara Pizzorno discusses the calcium paradox in a way you havent heard of before. Discover its initial reference and how it really isnt a paradox at all.
https://www.algaecal.com/expert-insights/calcium-paradox-its-history-and-what-it-really-means/
The Weekly Independent: April 12, 2021 - MBO PartnersThe Weekly Independent: April 12, 2021 - MBO Partners
News and notes for independent workers and their clients. This is the latest edition of The Weekly Independent from MBO Partners.
https://www.mbopartners.com/blog/weekly-independent/the-weekly-independent-april-12-2021/
MyoglobinMyoglobin
... is found in Type I muscle, Type II A, and Type II B; although many texts consider myoglobin not to be found in smooth ... All known vertebrate myoglobins and β-hemoglobin subunits are similar in structure, but myoglobin binds O2 more avidly at low ... Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not ... In humans, myoglobin is only found in the bloodstream after muscle injury. High concentrations of myoglobin in muscle cells ...
https://en.wikipedia.org/wiki/Myoglobin
Impossible FoodsImpossible Foods
"Hemoglobin and myoglobin". The Medical Biochemistry Page. 2020. Archived from the original on 2017-08-30. Retrieved 2017-08-29 ...
https://en.wikipedia.org/wiki/Impossible_Foods
GlobinGlobin
Myoglobin (Mb) Neuroglobin: a myoglobin-like haemprotein expressed in vertebrate brain and retina, where it is involved in ... The globin fold was thus the first protein fold discovered (myoglobin was the first protein whose structure was solved). The ... Two prominent members include myoglobin and hemoglobin. Both of these proteins reversibly bind oxygen via a heme prosthetic ... Eight globins are known to occur in vertebrates: androglobin, cytoglobin, globin E, globin X, globin Y, hemoglobin, myoglobin ...
https://en.wikipedia.org/wiki/Globin
Frederic M. RichardsFrederic M. Richards
Along with colleague Harold W. Wyckoff, who had worked on early research toward the myoglobin structure, the effort to solve ... Kendrew JC, Dickerson RE, Strandberg BE, Hart RG, Davies DR, Phillips DC, Shore VC (1960). "Structure of myoglobin: a three- ... Bodo G, Dintzis HM, Kendrew JC, Wyckoff HW (1959). "The crystal structure of myoglobin. V. A low resolution three-dimensional ... Two years later, the protein structure of myoglobin confirmed such specific 3D relationships. Later, with Marilyn Doscher and ...
https://en.wikipedia.org/wiki/Frederic_M._Richards
John KendrewJohn Kendrew
Whale myoglobin did give large crystals with clean X-ray diffraction patterns. However, the problem still remained ... Ingram, DJ; Kendrew, JC (October 1956). "Orientation of the haem group in myoglobin and its relation to the polypeptide chain ... Kendrew determined the structure of the protein myoglobin, which stores oxygen in muscle cells. On Saturday 20 October 1962 the ... Watson, HC; Kendrew, JC (May 1961). "The amino-acid sequence of sperm whale myoglobin. Comparison between the amino-acid ...
https://en.wikipedia.org/wiki/John_Kendrew
Striated muscle tissueStriated muscle tissue
They contain many mitochondria and myoglobin. Unlike skeletal muscle, cardiac muscle cells are unicellular. These cells are ...
https://en.wikipedia.org/wiki/Striated_muscle_tissue
Gerd Ulrich NienhausGerd Ulrich Nienhaus
"X-ray structure determination of a metastable state of carbonmonoxy myoglobin after photodissociation". Proceedings of the ... "Ligand binding and conformational motions in myoglobin". Nature. 404 (6774): 205-208. Bibcode:2000Natur.404..205O. doi:10.1038/ ...
https://en.wikipedia.org/wiki/Gerd_Ulrich_Nienhaus
1960 in science1960 in science
John Kendrew publishes the structure of myoglobin. March 5 - British marine biologist Sir Alister Hardy announces his aquatic ... 13 February 1960). "Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution". Nature. 185 (4711): 422- ...
https://en.wikipedia.org/wiki/1960_in_science
Laura EisensteinLaura Eisenstein
"Activation Energy Spectrum in Myoglobin---a Comment". Physical Review Letters. 34 (13): 845. Bibcode:1975PhRvL..34..845A. doi: ...
https://en.wikipedia.org/wiki/Laura_Eisenstein
Curing (food preservation)Curing (food preservation)
... because they bond to the myoglobin and act as a substitute for oxygen, thus turning myoglobin red. More recent evidence shows ... Ulin, Don (10 May 2011). "Why Meat Stays Red: Myoglobin And Nitrites". A Moment of Science - Indiana Public Media. Schweihofer ... which then binds to the iron atom in the center of myoglobin's heme group, reducing oxidation and causing a reddish-brown color ...
https://en.wikipedia.org/wiki/Curing_(food_preservation)
HemoproteinHemoprotein
Myoglobin is found in vertebrate muscle cells. Muscle cells, when put into action, can quickly require a large amount of oxygen ... Myoglobin and hemoglobin are globular proteins that serve to bind and deliver oxygen using a prosthetic group. These globins ... Myoglobin also stores the required amount of oxygen and makes it available for the muscle cell mitochondria. In vertebrates, ... It binds to the 6th coordination position of the iron, His-E7 of the myoglobin binds to the oxygen that is now covalently ...
https://en.wikipedia.org/wiki/Hemoprotein
WhaleWhale
... haemoglobin and myoglobin store oxygen in body tissue; and they have twice the concentration of myoglobin than haemoglobin. ... Norena, S. R.; Williams, T. M. (2000). "Body size and skeletal muscle myoglobin of cetaceans: adaptations for maximizing dive ...
https://en.wikipedia.org/wiki/Whale
CoboglobinCoboglobin
A coboglobin is a synthetic compound, a metalloprotein chemically similar to hemoglobin or myoglobin but using the metal cobalt ... Hoffman, B. M.; Petering, D. H (October 1970). "Coboglobins: Oxygen-Carrying Cobalt-Reconstituted Hemoglobin and Myoglobin". ... instead of iron (hence the name). Just like hemoglobin and myoglobin, the coboglobins are able to reversibly bind molecular ...
https://en.wikipedia.org/wiki/Coboglobin
Carbon monoxide poisoningCarbon monoxide poisoning
It has a high affinity for myoglobin, about 60 times greater than that of oxygen. Carbon monoxide bound to myoglobin may impair ... Additionally, many other hemoproteins such as myoglobin, Cytochrome P450, and mitochondrial cytochrome oxidase are affected, ... Known mechanisms include carbon monoxide binding to hemoglobin, myoglobin and mitochondrial cytochrome c oxidase and ... Carbon monoxide also binds to the hemeprotein myoglobin. ... may be due to a late release of carbon monoxide from myoglobin ...
https://en.wikipedia.org/wiki/Carbon_monoxide_poisoning
HallucinogenHallucinogen
... some deaths have been reported due to the release of myoglobin from ruptured muscle cells. High amounts of myoglobin can induce ...
https://en.wikipedia.org/wiki/Hallucinogen
Kristin Bowman-JamesKristin Bowman-James
Her doctoral research considers azado complexes as models for myoglobin. She spent a year as a postdoctoral Fellow at the Ohio ... Iron (II) complexes as models for myoglobin (Thesis). Philadelphia. "Distinguished chemistry professor Kristin Bowman-James ...
https://en.wikipedia.org/wiki/Kristin_Bowman-James
Serum ironSerum iron
About 4% is bound up in myoglobin molecules. Around 30% of the iron in the body is stored as ferritin or hemosiderin in the ...
https://en.wikipedia.org/wiki/Serum_iron
CetaceaCetacea
The muscle pigment, myoglobin, provides an effective bond. This additional oxygen storage is vital for deep diving, since ...
https://en.wikipedia.org/wiki/Cetacea
Toothed whaleToothed whale
... haemoglobin and myoglobin store oxygen in body tissue; and they have twice the concentration of myoglobin than haemoglobin. ... ISBN 978-0-521-44418-7. Norena, S. R.; Williams, T. M. (2000). "Body size and skeletal muscle myoglobin of cetaceans: ...
https://en.wikipedia.org/wiki/Toothed_whale
Tastes like chickenTastes like chicken
Myoglobin-rich meat is often called red meat. Burros, Marian (November 21, 2001). "The Hunt for a Truly Grand Turkey, One That ... The taste difference is usually attributed to low concentrations of the iron-containing protein myoglobin, a high concentration ...
https://en.wikipedia.org/wiki/Tastes_like_chicken
Nature (journal)Nature (journal)
First molecular protein structure (myoglobin) - J. C. Kendrew; G. Bodo; H. M. Dintzis; R. G. Parrish; H. Wyckoff; D. C. ... Phillips (1958). "A three-dimensional model of the myoglobin molecule obtained by X-ray analysis". Nature. 181 (4610): 662-666 ...
https://en.wikipedia.org/wiki/Nature_(journal)
Hypoxia in fishHypoxia in fish
Increased expression of myoglobin, which is normally only found in muscle tissue, has also been observed after hypoxia exposure ... "Hypoxia-inducible myoglobin expression in non-muscle tissues". Proc Natl Acad Sci USA. 103 (8): 2977-2981. doi:10.1073/pnas. ...
https://en.wikipedia.org/wiki/Hypoxia_in_fish
Hydrophobic effectHydrophobic effect
Callaway, David J. E. (1994). "Solvent-induced organization: a physical model of folding myoglobin". Proteins: Structure, ...
https://en.wikipedia.org/wiki/Hydrophobic_effect
Entropic forceEntropic force
Callaway, David J. E. (1994). "Solvent-induced organization: a physical model of folding myoglobin". Proteins: Structure, ...
https://en.wikipedia.org/wiki/Entropic_force
Facilitated diffusionFacilitated diffusion
Its affinity for myoglobin is 40 times higher and 250 times higher for hemoglobin, compared to oxygen. Since glucose is a large ... This mechanism of facilitated diffusion of oxygen by hemoglobin or myoglobin was discovered and initiated by Wittenberg and ... Rubinow SI, Dembo M (April 1977). "The facilitated diffusion of oxygen by hemoglobin and myoglobin". Biophys. J. 18 (1): 29-42 ... Carbon monoxide also combines with hemoglobin and myoglobin, but carbon monoxide has a dissociation velocity that 100 times ...
https://en.wikipedia.org/wiki/Facilitated_diffusion
Bioinorganic chemistryBioinorganic chemistry
Other oxygen transport systems include myoglobin, hemocyanin, and hemerythrin. Oxidases and oxygenases are metal systems found ...
https://en.wikipedia.org/wiki/Bioinorganic_chemistry
Stephen A. CusackStephen A. Cusack
subscription required) Doster, W; Cusack, S; Petry, W (1989). "Dynamical transition of myoglobin revealed by inelastic neutron ...
https://en.wikipedia.org/wiki/Stephen_A._Cusack
Titanate nanosheetTitanate nanosheet
Similarly, intercalated myoglobin is proven to be an efficient catalyst for H2O2. TiNSs may also be used for immobilizing ... Zhang, L.; Zhang, Q.; Li, J. (2007-07-12). "Layered Titanate Nanosheets Intercalated with Myoglobin for Direct Electrochemistry ...
https://en.wikipedia.org/wiki/Titanate_nanosheet
Crotalus durissusCrotalus durissus
Myoglobin released into the blood results in dark urine. Other serious complications may result from systemic disorders ( ...
https://en.wikipedia.org/wiki/Crotalus_durissus
TeleostTeleost
Brown, W. Duane (1962). "The concentration of myoglobin and hemoglobin in tuna flesh". Journal of Food Science. 27 (1): 26-28. ... and muscles with a raised myoglobin content, which gives these a reddish colour and makes for a more efficient use of oxygen. ...
https://en.wikipedia.org/wiki/Teleost
Myoglobin blood test: MedlinePlus Medical EncyclopediaMyoglobin blood test: MedlinePlus Medical Encyclopedia
The myoglobin blood test measures the level of the protein myoglobin in the blood. ... Serum myoglobin; Heart attack - myoglobin blood test; Myositis - myoglobin blood test; Rhabdomyolysis - myoglobin blood test ... Myoglobin is a protein in heart and skeletal muscles. When you exercise, your muscles use up available oxygen. Myoglobin has ... The kidneys help remove myoglobin from the blood into the urine. When the level of myoglobin is too high, it can damage the ...
https://medlineplus.gov/ency/article/003663.htm
Myoglobin - DocCheck FlexikonMyoglobin - DocCheck Flexikon
Myoglobin is a globular protein and consists of eight α-helixes in its secondary structure. Myoglobin is a protein composed of ... High myoglobin levels are nephrotoxic due to free iron that is released from myoglobin during degradation. Thereby, it can lead ... The hyperbolic binding curve is characteristic for myoglobin and distinguishes myoglobin from hemoglobin which has a sigmoidal ... Myoglobin (Mb) is a oxygen storage protein which belongs to the family of globins. It is present in the striated muscles and ...
https://flexikon.doccheck.com/en/Myoglobin
RCSB PDB - 109M: SPERM WHALE MYOGLOBIN D122N ETHYL ISOCYANIDE AT PH 9.0RCSB PDB - 109M: SPERM WHALE MYOGLOBIN D122N ETHYL ISOCYANIDE AT PH 9.0
SPERM WHALE MYOGLOBIN D122N ETHYL ISOCYANIDE AT PH 9.0 ... MYOGLOBIN. A. 154. Physeter catodon. Mutation(s): 1 Gene Names ... SPERM WHALE MYOGLOBIN D122N ETHYL ISOCYANIDE AT PH 9.0. *PDB DOI: 10.2210/pdb109M/pdb ... Correlations between Bound N-Alkyl Isocyanide Orientations and Pathways for Ligand Binding in Recombinant Myoglobins. Smith, R. ...
https://www.rcsb.org/structure/109m
Hemoglobin and Myoglobin in Urine in Cats | PetMDHemoglobin and Myoglobin in Urine in Cats | PetMD
Myoglobin serves the same purpose as hemoglobin but is particular to the muscles, and is differentiated by the amount of oxygen ... If there is too much hemoglobin and myoglobin in the blood plasma, these proteins will no longer be reabsorbed in the kidneys, ... Consequently, plasma color does not change, and the myoglobin is quickly cleared from the blood by the liver and kidneys. ... Not only can hemoglobin and myoglobin damage the kidneys, but their presence in the blood indicates low oxygen-carrying ...
https://www.petmd.com/cat/conditions/cardiovascular/c_ct_hemoglobinuria_myoglobinuria
Myoglobin (M8A), mAb, Mouse - GenScriptMyoglobin (M8A), mAb, Mouse - GenScript
Myoglobin (symbol Mb or MB) is an iron-and oxygen-binding protein. Its level in blood increases above normal levels at the ... Myoglobin (M8A), mAb, Mouse. Myoglobin (symbol Mb or MB) is an iron-and oxygen-binding protein. Its level in blood increases ... Myoglobin (symbol Mb or MB) is an iron-and oxygen-binding protein. Its level in blood increases above normal levels at the ... Myoglobin (symbol Mb or MB) is an iron-and oxygen-binding protein. Its level in blood increases above normal levels at the ...
https://www.genscript.com/antibody/V00503_1-Myoglobin_M8A_mAb_Mouse.html
Myoglobin Protein Human Recombinant | MB Antigen | ProSpecMyoglobin Protein Human Recombinant | MB Antigen | ProSpec
Myoglobin Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 17.67 kDa. ... Myoglobin is found in Type I muscle, Type II A and Type II B, but it is mostly deemed that myoglobin is not found in smooth ... Myoglobin, MB, PVALB, MGC13548.. Introduction. Myoglobin is a member of the globin superfamily and can be found in skeletal and ... Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobins molecular weight is 16.7 kDa, and it is the primary oxygen- ...
https://www.prospecbio.com/myoglobin_human_recombinant
Rabbit Myoglobin MYO ELISA Kit - Gentaur.comRabbit Myoglobin MYO ELISA Kit - Gentaur.com
... - Product info ... MYO ELISA Kit, Rat Myoglobin ELISA Kit. Catalog number:EF017901 ...
https://gentaur.com/enlibio/rabbit-myoglobin-myo-elisakit-01017007188
Rat MYO (Myoglobin) ELISA Kit | G-EC-05116 | Gentaur Elisa KitsRat MYO (Myoglobin) ELISA Kit | G-EC-05116 | Gentaur Elisa Kits
Myoglobin) ELISA Kit from Gentaur Elisa Kits. Cat Number: G-EC-05116. USA, UK & Europe Distribution. ... Rat MYO (Myoglobin) ELISA Kit , G-EC-05116. Rating * Select Rating. 1 star (worst). 2 stars. 3 stars (average). 4 stars. 5 ...
https://caslab.com/rat-myo-myoglobin-elisa-kit-g-ec-05116/
SciELO - Brazil - Immobilization of myoglobin in sodium alginate composite membranes Immobilization of myoglobin in sodium...SciELO - Brazil - Immobilization of myoglobin in sodium alginate composite membranes Immobilization of myoglobin in sodium...
Immobilization of myoglobin in sodium alginate composite membranes Katia Cecília de Souza Figueiredo Instituto Alberto Luiz ... The spectra for myoglobin solutions containing calcium and iron chloride at 20°C are presented on Figures 4a and b. The ... 2.2 Myoglobin activation. Metmyoglobin (Fe3+) was activated, i. e., reduced to Fe2+, by reacting the protein aqueous solution ... As myoglobin is positively charged in the pH of 6.5, it could work as an ionic crosslinker for SA membranes. However, the ...
https://www.scielo.br/j/po/a/sBNnrdvZB7CzTtwxznYx9xw/?lang=en
Recombinant Human Myoglobin
Online Myoglobin Urine Test | Affordable Myoglobin Urine Test | Request A TestOnline Myoglobin Urine Test | Affordable Myoglobin Urine Test | Request A Test
Increased myoglobin in the urine could be a sign of kidney failure or a serious muscle injury. Take charge of your health by ... Myoglobin Urine Test (Labcorp). This test measures Myoglobin levels in the urine. Myoglobin is a protein that helps provide ... Myoglobin Urine Test (Quest). This test measures Myoglobin levels in the urine. Myoglobin is a protein that helps provide ... Myoglobin Urine Test (Labcorp). This test measures Myoglobin levels in the urine. Myoglobin is a protein that helps provide ...
https://requestatest.com/myoglobin-urine-test
A circular dichroism study of the protective role of polyphosphoesters polymer chains in polyphosphoester-myoglobin conjugates ...A circular dichroism study of the protective role of polyphosphoesters polymer chains in polyphosphoester-myoglobin conjugates ...
The influence of pH and salts on the A-states of myoglobinThe influence of pH and salts on the A-states of myoglobin
... Mueller, Joachim D.; McMahon, Ben; Nienhaus, G. Ulrich. ...
https://publikationen.bibliothek.kit.edu/1000057321
Abstract PS19-17: The role of myoglobin in breast cancer | Cancer Research | American Association for Cancer ResearchAbstract PS19-17: The role of myoglobin in breast cancer | Cancer Research | American Association for Cancer Research
Abstract PS19-17: The role of myoglobin in breast cancer Mostafa A. Aboouf; Mostafa A. Aboouf ... The role of myoglobin in breast cancer [abstract]. In: Proceedings of the 2020 San Antonio Breast Cancer Virtual Symposium; ... Recently, our group co-discovered myoglobin (MB) to be expressed in luminal cells of healthy and cancerous breast epithelia of ... However, if and how myoglobin itself restricts mammary tumorigenesis is completely unclear. To understand how MB exerts its ...
https://aacrjournals.org/cancerres/article/81/4_Supplement/PS19-17/648478/Abstract-PS19-17-The-role-of-myoglobin-in-breast
Myoglobin, Serum | Ulta Lab TestsMyoglobin, Serum | Ulta Lab Tests
The Myoglobin, Serum Quest lab test contains 1 test with 1 biomarker. ... Myoglobin, Serum Most Popular. The Myoglobin, Serum test contains 1 test with 1 biomarker. ... Myoglobin, Serum #660 1 Biomarkers - Specimen Type: Serum - Average Process Time*: 3 to 4 days ...
https://www.ultalabtests.com/test/myoglobin-serum
T cell response to myoglobin: a comparison of T cell clones in high‐responder and low‐responder mice<...
Gorai I, Aihara M, Bixler GS, Zouhair Atassi M, Walden P, Klein J. T cell response to myoglobin: a comparison of T cell clones ... T cell response to myoglobin : a comparison of T cell clones in high‐responder and low‐responder mice. In: European Journal of ... Mice carrying the H‐2b haplotype (e.g., inbred strains C57BL/6 and C57BL/10) are low responders to sperm whale myoglobin when ... Gorai, I, Aihara, M, Bixler, GS, Zouhair Atassi, M, Walden, P & Klein, J 1988, T cell response to myoglobin: a comparison of T ...
https://pennstate.pure.elsevier.com/en/publications/t-cell-response-to-myoglobin-a-comparison-of-t-cell-clones-in-hig
Viana | Thermal Instability Induced by 4-Hydroxy-2-Nonenal in Beef Myoglobin | Meat and Muscle BiologyViana | Thermal Instability Induced by 4-Hydroxy-2-Nonenal in Beef Myoglobin | Meat and Muscle Biology
Keywords: beef myoglobin, redox stability, mass spectrometry, thermal stability, lipid oxidation. How to Cite: Viana, F. M. & ... Redox instability induced by 4-hydroxy-2-nonenal in porcine and bovine myoglobins at pH 5.6 and 4 °C. J. Agr. Food Chem. 54: ... Percentage myoglobin denaturation (PMD) in beef oxymyoglobin (OMb; 0.15 mM) at 71°C, after incubation with 4-hydroxy-2-nonenal ... Thermal Instability Induced by 4-Hydroxy-2-Nonenal in Beef Myoglobin. Authors *Fernanda M. Viana (University of Kentucky) ...
https://iastatedigitalpress.com/mmb/article/id/9479/
ARCHITECT MYOGLOBIN CTL(1 EA)ARCHITECT MYOGLOBIN CTL(1 EA)
... *Use the PRINT, EMAIL and PDF buttons, to the right, to share only this page. To share the full ...
https://www.e-abbott.com/architect-myoglobin-ctl-1-ea.html
Myoglobin: An Example of Protein StructureMyoglobin: An Example of Protein Structure
... In many ways, myoglobin is the classic example of a globular protein. We shall use ... Myoglobin has eight α-helical regions and no β-pleated sheet regions. Approximately 75% of the residues in myoglobin are found ... The myoglobin molecule (including the heme group) has a compact structure, with the interior atoms very close to each other. ... The complete myoglobin molecule consists of a single polypeptide chain of 153 amino acid residues and includes a prosthetic ...
https://www.brainkart.com/article/Myoglobin--An-Example-of-Protein-Structure_27472/
Acute Coronary Syndrome Workup: Approach Considerations, Electrocardiography, Measurement of CK-MB LevelsAcute Coronary Syndrome Workup: Approach Considerations, Electrocardiography, Measurement of CK-MB Levels
Measurement of Myoglobin Levels. Myoglobin is not cardiac specific, but it may be detected as early as 2 hours after myocardial ... Myoglobin values have a high negative predictive value when blood is sampled in the first 4-8 hours after onset. ... However, myoglobin results should be supplemented with other, more specific cardiac biomarkers, such as CK-MB or troponin. ... Peak A is the early release of myoglobin or creatine kinase isoenzyme MB (CK-MB) after acute myocardial infarction (AMI). Peak ...
https://www.medscape.com/answers/1910735-178341/what-is-the-role-of-biomarkers-in-the-workup-of-acute-coronary-syndrome-acs
John Kendrew First Applies an Electronic Computer to Molecular or Structural Biology to Calculate Structure Factors of...John Kendrew First Applies an Electronic Computer to Molecular or Structural Biology to Calculate Structure Factors of...
Kendrew First Applies an Electronic Computer to Molecular or Structural Biology to Calculate Structure Factors of Myoglobin ... In 1962 Kendrew received the Nobel Prize in chemistry for his discovery of the 3-dimensional molecular structure of myoglobin, ... EDSAC for the computation of Fourier syntheses in the calculation of structure factors of the protein molecule myoglobin. This ... Kendrew First Applies an Electronic Computer to Molecular or Structural Biology to Calculate Structure Factors of Myoglobin. 7/ ...
https://historyofinformation.com/detail.php?entryid=894
Acute Coronary Syndrome Workup: Approach Considerations, Electrocardiography, Measurement of CK-MB LevelsAcute Coronary Syndrome Workup: Approach Considerations, Electrocardiography, Measurement of CK-MB Levels
Measurement of Myoglobin Levels. Myoglobin is not cardiac specific, but it may be detected as early as 2 hours after myocardial ... Myoglobin values have a high negative predictive value when blood is sampled in the first 4-8 hours after onset. ... However, myoglobin results should be supplemented with other, more specific cardiac biomarkers, such as CK-MB or troponin. ... Peak A is the early release of myoglobin or creatine kinase isoenzyme MB (CK-MB) after acute myocardial infarction (AMI). Peak ...
http://emedicine.medscape.com/article/1910735-workup
MyoglobinMyoglobin
... Human. Human Myoglobin produced in Human Cardiac Tissues having a molecular mass of 17.5kDa. Myoglobin is released ... Myoglobin Human. Myoglobin Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass ... The Myoglobin is purified by proprietary chromatographic techniques.. 10µg. 50µg. 1mg. $65. Add to Cart ... Myoglobin His Human. MB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154a.a ...
https://neobiolab.com/myoglobin
Myoglobin - AccuteqsMyoglobin - Accuteqs
All material on this website is provided for your information only and may not be construed as medical advice or instruction. No action or inaction should be taken based solely on the contents of this information; instead, readers should consult appropriate health professionals on any matter relating to their health and well-being. The information provided is not intended to be a substitute for professional medical advice, diagnosis or treatment. Never disregard professional medical advice, or delay in seeking it, because of something you have read on this website. Never rely on the information on this website in place of seeking professional medical advice. Accuteqs.com.ph is not responsible or liable for any advice, course of treatment, diagnosis or any other information, services or products that you obtain through this site.. ...
https://accuteqs.com.ph/myoglobin/
Myoglobin - CellSystems®Myoglobin - CellSystems®
Supplier for Enzymes - Benefit from a regular stock of 10000 or more products and a shipping time of 24 hours.
https://cellsystems.eu/product/myoglobin/
MYOGLOBIN, URINE - Bio DiagnosticMYOGLOBIN, URINE - Bio Diagnostic
MYOGLOBIN, URINE. Lorem Ipsum is simply dummy text of the printing and typesetting industry. Lorem Ipsum has been the ...
http://biodiagnostic.co.in/myoglobin-urine/
Myoglobin Archives - Medical ActuMyoglobin Archives - Medical Actu
Markers infartus infarction - myoglobin, troponin and isoenzyme of creatine kinase. Dr. Taoufik - 27 October 2016. 1 ...
https://www.medical-actu.com/en/tag/myoglobin/
IMSEAR at SEARO: Clinical significance of urine myoglobin in high voltage electrical burns.
Clinical significance of urine myoglobin in high voltage electrical burns.. Authors: Narayan, G Amar Raghu. Deepthi, S K. Singh ... The present study was conducted to evaluate the role of urine myoglobin in the early prediction of acute renal failure in ... Whereas urine myoglobin levels were deranged in all twenty one patients with high voltage electrical burns. ... Clinical significance of urine myoglobin in high voltage electrical burns. International Journal of Applied Biology and ...
https://imsear.searo.who.int/handle/123456789/164143
Myoglobin Test @1000 | Home Sample CollectionMyoglobin Test @1000 | Home Sample Collection
Myoglobin can also be measured with a urine test. ... The myoglobin blood test measures the level of the protein ...
https://www.indushealthplus.com/lab-packages/myoglobin.html
Horse heart myoglobinSerumHemoglobin and myoglobinProteinKidneysReleased into the bloodstreamSperm whale myoglobinRhabdomyolysisHemePurified by proprietary chromatographic techniquesMoleculePeptidesProteinsAcuteMusclesSignificance of urineTissuesRedoxRecombinantCardiacMeatMyopathyUrine testDegradationConcentrationsMyocardial ischemiaMetabolismMuscle tissueZincBind oxygenMembraneBloodTestLevelsAbstractIncreasesHighHeart
Horse heart myoglobin3
  • Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. (wikidata.org)
  • Multilayer thin films of ∼ 7 nm diameter gold nanoparticles (GNPs) linked with horse heart myoglobin (Mb) are fabricated, for the first time, by layer-by-layer (LbL) assembly on glass slides, and silicon and plastic substrates. (elsevier.com)
  • Accordingly, CoQ1H2 and CoQ2H2 effectively prevented tyrosyl radical-dependent reactions such as the dimerization of sperm whale myoglobin and heme-apoprotein covalent binding in horse heart myoglobin. (unicatt.it)
Serum3
  • Muscle damage releases myoglobin into the blood plasma, but it does not bind to serum proteins. (petmd.com)
  • The Myoglobin, Serum test contains 1 test with 1 biomarker. (ultalabtests.com)
  • Study includes 21 patients of high volatage electrical burns underwent four different Renal parameters i.e blood urea, serum creatinine, serum potassium and urine myoglobin levels. (who.int)
Hemoglobin and myoglobin3
  • If there is too much hemoglobin and myoglobin in the blood plasma, these proteins will no longer be reabsorbed in the kidneys, and will instead spill over into the urine. (petmd.com)
  • Not only can hemoglobin and myoglobin damage the kidneys, but their presence in the blood indicates low oxygen-carrying capacity, which can result in liver damage, serious illness, and shock, all of which serve to further decrease the amount of oxygen available through the muscles and blood. (petmd.com)
  • It is also important to remember that although our metabolism requires that hemoglobin and myoglobin bind oxygen, it would be equally disastrous if the heme never let the oxygen go. (brainkart.com)
Protein15
  • The myoglobin blood test measures the level of the protein myoglobin in the blood. (medlineplus.gov)
  • Myoglobin is a protein in heart and skeletal muscles. (medlineplus.gov)
  • Myoglobin (Mb) is a oxygen storage protein which belongs to the family of globins . (doccheck.com)
  • Myoglobin is a globular protein and consists of eight α-helixes in its secondary structure. (doccheck.com)
  • Myoglobin is a protein composed of a single polypeptide chain build by 153 amino acids. (doccheck.com)
  • Myoglobin (symbol Mb or MB) is an iron-and oxygen-binding protein. (genscript.com)
  • The immobilization of myoglobin in sodium alginate films was investigated with the aim of evaluating the protein stability in an ionic polymeric matrix. (scielo.br)
  • The electrostatic interaction between the protein and the polysaccharide did not damage the UV-visible pattern of native myoglobin. (scielo.br)
  • Myoglobin is a protein that helps provide oxygen to the heart and skeletal muscles allowing them to function properly. (requestatest.com)
  • Cooked color is primarily dictated by the heat-induced denaturation of myoglobin (Mb), which is the sarcoplasmic heme protein responsible for fresh meat color. (iastatedigitalpress.com)
  • In many ways, myoglobin is the classic example of a globular protein. (brainkart.com)
  • Myoglobin was the first protein for which the complete tertiary structure (Figure 4.15) was determined by X-ray crystallography. (brainkart.com)
  • At the second English computer conference held in Manchester from July 9-12, 1951 computer scientist John Makepiece Bennett and biochemist and crystallographer John Kendrew described their use of the Cambridge EDSAC for the computation of Fourier syntheses in the calculation of structure factors of the protein molecule myoglobin . (historyofinformation.com)
  • In 1962 Kendrew received the Nobel Prize in chemistry for his discovery of the 3-dimensional molecular structure of myoglobin , the first protein molecule to be "solved. (historyofinformation.com)
  • We have investigated the photoinduced electron transfer (ET) in the 1:1 cross-linked complex (CL-ZnMb/b 5 ) formed by a cross-linking reagent, EDC, between Zn-substituted myoglobin (ZnMb) and cytochrome b 5 (Cytb 5 ) to reveal the mechanism of the inter-protein ET reactions under the condition of multiple encounter complexes. (elsevier.com)
Kidneys8
  • The kidneys help remove myoglobin from the blood into the urine. (medlineplus.gov)
  • When the level of myoglobin is too high, it can damage the kidneys. (medlineplus.gov)
  • Consequently, plasma color does not change, and the myoglobin is quickly cleared from the blood by the liver and kidneys. (petmd.com)
  • Even though the released myoglobin is filtered by the kidneys, it is toxic to the renal tubular epithelium and thus may cause acute renal failure. (prospecbio.com)
  • Myoglobin is filtered out of the blood by the kidneys and excreted from the body in urine. (requestatest.com)
  • Too much myoglobin can cause damage to the kidneys. (requestatest.com)
  • Physical activity in hot conditions causes breakdown of skeletal muscle tissue, releasing chemicals such as myoglobin that harm the kidneys' internal structures. (cdc.gov)
  • At that point, the built up of toxins and myoglobin head to the kidneys where they block the kidneys. (lsbeckerlaw.com)
Released into the bloodstream3
  • When muscle is damaged, myoglobin in muscle cells is released into the bloodstream. (medlineplus.gov)
  • If the heart or skeletal muscles are damaged, myoglobin is released into the bloodstream. (requestatest.com)
  • it was a hemoglobin cousin, myoglobin, the oxygen-​carrying component of muscle, which is released into the bloodstream after an injury. (innovatiomedia.com)
Sperm whale myoglobin1
  • Mice carrying the H‐2 b haplotype (e.g., inbred strains C57BL/6 and C57BL/10) are low responders to sperm whale myoglobin when tested in the T cell proliferation assay. (elsevier.com)
Rhabdomyolysis3
  • Any situation that leads to rhabdomyolysis increases myoglobin values in the blood. (doccheck.com)
  • Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. (prospecbio.com)
  • The urine myoglobin for rhabdomyolysis. (cdc.gov)
Heme7
  • The polypeptide chain is bound to a heme molecule which represents the prosthetic group of myoglobin. (doccheck.com)
  • The heme is bound to a histidine residue at position 93 (His93 or His-F8) within the N-terminal end of the myoglobin polypeptide. (doccheck.com)
  • Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. (prospecbio.com)
  • The complete myoglobin molecule consists of a single polypeptide chain of 153 amino acid residues and includes a prosthetic group, the heme group, which also occurs in hemoglobin. (brainkart.com)
  • The myoglobin molecule (including the heme group) has a compact structure, with the interior atoms very close to each other. (brainkart.com)
  • The pres-ence of the heme group is required for myoglobin to bind oxygen. (brainkart.com)
  • The Myoglobin heme free contains N-terminal T7 tag and purified by proprietary chromatographic techniques. (neobiolab.com)
Purified by proprietary chromatographic techniques1
  • The Myoglobin is purified by proprietary chromatographic techniques. (prospecbio.com)
Molecule2
  • To determine whether T cells from the low and high‐responder mice recognize the same or different epitopes on the immunizing antigen, we obtained sets of T cell clones from both strains and tested them against peptides representing different regions of the myoglobin molecule, as well as against myoglobins from species other than the sperm whale. (elsevier.com)
  • Iron is an essential component of hemoglobin, a molecule that transports oxygen to the cells of the body, and myoglobin, which binds oxygen used in muscle tissues. (procarenow.com)
Peptides1
  • and 2 types did not respond to any of the peptides used (1 type, but not the other, responded to dog myoglobin). (elsevier.com)
Proteins2
  • The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only. (prospecbio.com)
  • Bilirubin is a metabolite of haem, derived from haem-containing proteins, including myoglobin, haemoglobin and various P450 enzymes, that serves to coordinate iron in various proteins. (randox.com)
Acute3
  • Peak A is the early release of myoglobin or creatine kinase isoenzyme MB (CK-MB) after acute myocardial infarction (AMI). (medscape.com)
  • The present study was conducted to evaluate the role of urine myoglobin in the early prediction of acute renal failure in electrical burns. (who.int)
  • Acute renal failure can result from massive deposition of muscle enzymes and myoglobin in the renal tubules. (medscape.com)
Muscles6
  • Myoglobin has oxygen attached to it, which provides extra oxygen for the muscles to keep at a high level of activity for a longer period. (medlineplus.gov)
  • Myoglobin serves the same purpose as hemoglobin but is particular to the muscles, and is differentiated by the amount of oxygen and carbon monoxide it delivers to the tissues (more, and less, respectively). (petmd.com)
  • Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. (prospecbio.com)
  • Exercised muscles are darker in color, also due to myoglobin. (smartfoodsolutions.org)
  • In the human body, iron is present in all cells and has several vital functions -- as a carrier of oxygen to the tissues from the lungs in the form of hemoglobin (Hb), as a facilitator of oxygen use and storage in the muscles as myoglobin, as a transport medium for electrons within the cells in the form of cytochromes, and as an integral part of enzyme reactions in various tissues. (cdc.gov)
  • According to this article at Mercola, it is actually myoglobin, which is used to bring oxygen to muscles. (365daysofme.com)
Significance of urine2
  • IMSEAR at SEARO: Clinical significance of urine myoglobin in high voltage electrical burns. (who.int)
  • Nephrotoxicity of myoglobin within the rat: relative significance of urine pH and prior dehydration. (edu.hk)
Tissues1
  • Human Myoglobin produced in Human Cardiac Tissues having a molecular mass of 17.5kDa. (neobiolab.com)
Redox1
  • The secondary products of lipid oxidation, such as 4-hydroxy-2-nonenal (HNE), compromise myoglobin (Mb) redox stability and can thus impact thermal stability. (iastatedigitalpress.com)
Recombinant1
  • Myoglobin Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 17.67 kDa. (prospecbio.com)
Cardiac3
  • This preparation of Myoglobin is isolated from human cardiac muscle and is provided as a liquid in 20 mM Tris, 1 mM EDTA, 50% Glycerol, pH 8.5. (scrippslabs.com)
  • Enhanced fluorescence on silver island films (SIFs) is utilized to develop a sandwich-format immunoassay for the cardiac marker myoglobin (Myo). (unthsc.edu)
  • The cardiac troponins, in particular, have become the cardiac markers of choice for patients with ACS, eclipsing CK-MB and myoglobin in terms of clinical value. (medscape.com)
Meat3
  • Myoglobin is responsible for the pigments that make meat red. (prospecbio.com)
  • The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. (prospecbio.com)
  • Meat from mature animals is dark in color because myoglobin. (smartfoodsolutions.org)
Myopathy1
  • Follow CK and urine myoglobin for 36 hours myopathy (e.g., muscular dystrophy) at least. (medscape.com)
Urine test1
Degradation2
  • High myoglobin levels are nephrotoxic due to free iron that is released from myoglobin during degradation. (doccheck.com)
  • Approximately 75% of bilirubin is derived from hemoglobin, but degradation of myoglobin, cytochromes, and catalase also contributes. (medscape.com)
Concentrations2
  • Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. (prospecbio.com)
  • The initial results show that it is possible to detect Myoglobin concentrations below 50 ng/mL, which is lower than clinical cut-off for Myoglobin in healthy patients. (unthsc.edu)
Myocardial ischemia1
  • An increase of myoglobin levels is an unspecific marker for myocardial ischemia but a specific one for muscle injuries. (doccheck.com)
Metabolism1
  • In addition, myoglobin facilitates oxygen diffusion in muscle fibers that depend on aerobic metabolism. (training4cyclists.com)
Muscle tissue1
  • The other 15% is in the myoglobin of muscle tissue. (cdc.gov)
Zinc1
  • Post-Crystal Engineering of Zinc-Substituted Myoglobin to Construct a Long-Lived Photoinduced Charge-Separation System. (expasy.org)
Bind oxygen1
  • Myoglobin has a six times higher affinity to bind oxygen than hemoglobin. (doccheck.com)
Membrane1
  • The top layer of the dense composite membrane successfully immobilized Myoglobin, retaining the native UV-visible pattern for two months. (scielo.br)
Blood3
  • Your doctor will also probably take a blood smear to look for irregularities of the red blood cells, and may also use the ammonium sulfate test to detect hemoglobin or myoglobin presence in the blood. (petmd.com)
  • Urine testing is often ordered along with or as a follow up to a Myoglobin Blood Test . (requestatest.com)
  • [ 1 ] Urine dipstick reveals positive results for blood but no red cells, owing to the presence of myoglobin. (medscape.com)
Test3
Levels4
  • Whereas urine myoglobin levels were deranged in all twenty one patients with high voltage electrical burns. (who.int)
  • Myoglobin (MB) is not only strongly expressed in myocytes, but also at much lower levels in different cancer entities. (uni-mainz.de)
  • Myoglobin levels not measured at the right time may produce a false-negative result, though a positive result may help confirm the diagnosis. (medscape.com)
  • Paraoxonase-1 55 LL Genotype Is Associated with No ST-Elevation Myocardial Infarction and with High Levels of Myoglobin. (cdc.gov)
Abstract1
Increases1
High1
Heart1
  • Myoglobin testing may be ordered when someone is suspected of having a severe muscle injury or suffering a heart attack. (requestatest.com)
Acute Coronary Syndrome Workup: Approach Considerations, Electrocardiography, Measurement of CK-MB Levels
Acute Coronary Syndrome Workup: Approach Considerations, Electrocardiography, Measurement of CK-MB Levels (medscape.com)
Cardiac Markers: Definition and Efficacy, Markers of Myocardial Necrosis and Ischemia, Acute Coronary Syndrome Testing Strategy
Cardiac Markers: Definition and Efficacy, Markers of Myocardial Necrosis and Ischemia, Acute Coronary Syndrome Testing Strategy (medscape.com)
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Ck Mb Test, Myoglobin Test, Troponin Test - Laihe Biotech (lyherbio.com)
Examen de mioglobina en sangre: MedlinePlus enciclopedia médica
Examen de mioglobina en sangre: MedlinePlus enciclopedia médica (medlineplus.gov)
Acute Compartment Syndrome: Practice Essentials, Anatomy, Pathophysiology
Acute Compartment Syndrome: Practice Essentials, Anatomy, Pathophysiology (medscape.com)
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Myopathies Workup: Laboratory Studies, Other Tests (medscape.com)
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Acute Coronary Syndrome: Practice Essentials, Background, Etiology (medscape.com)
Poisoning Associated with Consumption of a Homemade Medicinal Liquor - Chongqing, China, 2018 | MMWR
Poisoning Associated with Consumption of a Homemade Medicinal Liquor - Chongqing, China, 2018 | MMWR (cdc.gov)
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Myoglobin - DocCheck Flexikon (flexikon.doccheck.com)
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3ase.1 | SWISS-MODEL Template Library (swissmodel.expasy.org)
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RCSB PDB - 109M: SPERM WHALE MYOGLOBIN D122N ETHYL ISOCYANIDE AT PH 9.0 (rcsb.org)
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Clinical Chemistry and Laboratory Medicine (CCLM) Volume 30 Issue 12 (degruyter.com)
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Toxins | Free Full-Text | Wound Infections of Snakebites from the Venomous Protobothrops mucrosquamatus and Viridovipera... (mdpi.com)
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Leghämoglobin - Wikipedia (de.wikipedia.org)
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Coronavirus Disease 2019 (COVID-19) in Children: Practice Essentials, Background, Pathophysiology (medscape.com)
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Hemoglobinopathy Retinopathy: Background, Pathophysiology, Epidemiology (medscape.com)
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Hyperkalemia Workup: Approach Considerations, Potassium Assay, Electrocardiography (medscape.com)
Sudden Cardiac Death: Practice Essentials, Background, Pathophysiology
Sudden Cardiac Death: Practice Essentials, Background, Pathophysiology (emedicine.medscape.com)
Symptoms: Rhabdomyolysis | NIOSH | CDC
Symptoms: Rhabdomyolysis | NIOSH | CDC (cdc.gov)
Brody myopathy: MedlinePlus Genetics
Brody myopathy: MedlinePlus Genetics (medlineplus.gov)
Rhabdomyolysis Workup: Approach Considerations, Laboratory Tests, Radiography, CT, and MRI
Rhabdomyolysis Workup: Approach Considerations, Laboratory Tests, Radiography, CT, and MRI (medscape.com)
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Myocardial Infarction Workup: Approach Considerations, Cardiac Biomarkers/Enzymes, Troponin Levels (emedicine.medscape.com)
(emedicine.medscape.com)
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Emergent Treatment of Gas Gangrene Workup: Laboratory Studies, Imaging Studies, Other Tests (emedicine.medscape.com)
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