A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
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.
Myoglobin which is in the oxidized ferric or hemin form. The oxidation causes a change in color from red to brown.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
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.
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)
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 (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)
Necrosis or disintegration of skeletal muscle often followed by myoglobinuria.
Chemical bond cleavage reactions resulting from absorption of radiant energy.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
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.
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
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.
Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.
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.
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.
Large mammals in the family Elephantidae, with columnar limbs, bulky bodies, and elongated snouts. They are the only surviving members of the PROBOSCIDEA MAMMALS.
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).
An essential amino acid that is required for the production of HISTAMINE.
A potent liver poison. In rats, bromotrichloromethane produces about three times the degree of liver microsomal lipid peroxidation as does carbon tetrachloride.
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.
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)
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
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.
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)
The rate dynamics in chemical or physical systems.
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)
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.
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.
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.
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).
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).
Community health education events focused on prevention of disease and promotion of health through audiovisual exhibits.
An activity in which the organism plunges into water. It includes scuba and bell diving. Diving as natural behavior of animals goes here, as well as diving in decompression experiments with humans or animals.
A syndrome related to increased atmospheric pressure and characterized by tremors, nausea, dizziness, decreased motor and mental performance, and SEIZURES. This condition may occur in those who dive deeply (c. 1000 ft) usually while breathing a mixture of oxygen and helium. The condition is associated with a neuroexcitatory effect of helium.
The study of natural phenomena by observation, measurement, and experimentation.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
The non-genetic biological changes of an organism in response to challenges in its ENVIRONMENT.
The study of those aspects of energy and matter in terms of elementary principles and laws. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Time period from 1801 through 1900 of the common era.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
Time period from 1901 through 2000 of the common era.
A surgical specialty which utilizes medical, surgical, and physical methods to treat and correct deformities, diseases, and injuries to the skeletal system, its articulations, and associated structures.
A syndrome characterized by the acute onset of unilateral FACIAL PARALYSIS which progresses over a 2-5 day period. Weakness of the orbicularis oculi muscle and resulting incomplete eye closure may be associated with corneal injury. Pain behind the ear often precedes the onset of paralysis. This condition may be associated with HERPESVIRUS 1, HUMAN infection of the facial nerve. (Adams et al., Principles of Neurology, 6th ed, p1376)
A group of adenine ribonucleotides in which the phosphate residues of each adenine ribonucleotide act as bridges in forming diester linkages between the ribose moieties.
The act or practice of calling public attention to a product, service, need, etc., especially by paid announcements in newspapers, magazines, on radio, or on television. (Random House Unabridged Dictionary, 2d ed)
Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.
A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.
The portion of an interactive computer program that issues messages to and receives commands from a user.
Sequential operating programs and data which instruct the functioning of a digital computer.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.

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)

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 ...
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 ...
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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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
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
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.. ...
Bio-Rad Antibodies (formerly AbD Serotec) is the research antibody division of Bio-Rad, the worlds leading life science company.
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Iron atom in PDB 2nsr: Nitromethane Modified Horse Heart Myoglobin
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 ...
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 ...
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 ...
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. ...
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. ...
AlphaLISA no-wash assay kit for detection and quantitation of Human Myoglobin in serum, buffered solution or cell culture medium.
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 ...
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. ...
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
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 ...
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 ...
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 ...
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. ...
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
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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
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
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 ...
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. ...
The extent of glycation and conformational changes of horse myoglobin (Mb) upon glycation with N-acetyl-glucosamine (GlcNAc), glucose...
Is there a relation between myocardial salvage and the release patterns of myoglobin and creatine kinase-MB in acute myocardial infarction submitted to thrombolysic ...
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 ...
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 ...
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 - ...
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. ...
what is the difference in the chemical structures of hemoglobin and myoglobin? Both consist of the same heme complex and a binded protein correct ...
what is the difference in the chemical structures of hemoglobin and myoglobin? Both consist of the same heme complex and a binded protein correct ...
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
Check out this lesson on the hemoglobin & myoglobin & learn everything you will need to know on for Pre-Nursing. View the lesson today!
View Notes - Hemoglobin Notes from CH 369 at University of Texas. Myoglobin,anoxygenbindingprotein Hasapolypeptidechainwithanironcontaininghemegroup.
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 ...
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
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 - ...
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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。
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 ...
1MNK: Interactions among residues CD3, E7, E10, and E11 in myoglobins: attempts to simulate the ligand-binding properties of Aplysia myoglobin.
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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 ...
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. ...
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 ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Iron atom in PDB 2zt2: Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser on [600 Min]
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 ...
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 ...
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 ...
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 ...
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 ...
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
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. ...
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%). ...
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 ...
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 ...
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 ...
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.
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 ...
Bronder, Helen S., Low Frequency Resonance Raman Study of Myoglobin Derivatives (1992). Masters Theses (1922-2009) Access restricted to Marquette Campus. 2441 ...
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 ...
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 ...
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 ...
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 ...
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.
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 ...
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. ...
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 ...
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 ...
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 ...
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 ...
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.. ...
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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 ...
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.
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.. ...
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 ...
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 ...
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 ...
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
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).. ...
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 ...
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 ...
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 ...
Near rhymes (words that almost rhyme) with rubin: blueprint, highfalutin, newsprint, myoglobin... Find more near rhymes/false rhymes at B-Rhymes.com
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.
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"Hemoglobin and myoglobin". The Medical Biochemistry Page. 2020. Archived from the original on 2017-08-30. Retrieved 2017-08-29 ...
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 ...
Lecture - 12 Myoglobin and Hemoglobin on YouTube *^ Biochemistry (Eighth ed.). New York: W. H. Freeman. 2015-04-08. ISBN ... Chen H, Ikeda-Saito M, Shaik S (2008). "Nature of the Fe-O2 bonding in oxy-myoglobin: effect of the protein". Journal of the ... Myoglobin. Found in the muscle tissue of many vertebrates, including humans, it gives muscle tissue a distinct red or dark gray ... Such a name is given because this arrangement is the same folding motif used in other heme/globin proteins such as myoglobin.[ ...
Well exercised muscles can not only add more size but can also develop more mitochondria, myoglobin, glycogen and a higher ... Type I fibers appear red due to the high levels of myoglobin. Red muscle fibers tend to have more mitochondria and greater ... They contain high mitochondrial volumes, and the high levels of myoglobin that give them a red pigmentation. They have been ... Traditionally, fibers were categorized depending on their varying color, which is a reflection of myoglobin content. ...
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 ...
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 ...
They contain many mitochondria and myoglobin. Unlike skeletal muscle, cardiac muscle cells are unicellular. These cells are ...
The color change is due to changes in the oxidation of the iron atom of the heme group in the myoglobin protein: raw meat is ... As meat is cooked, it turns from red to pink to gray to brown to black (if burnt), and the amount of red liquid, myoglobin (not ... red due to myoglobin protein in the muscles, not hemoglobin from blood (which also contains a heme group, hence the color). ...
Myoglobin. (talk , contribs)‎ (Undid revision 820646265 by 176.74.176.148 (talk)Undoing vandalism) (Tag: Undo) ... talk , contribs)‎ (Reverting possible vandalism by 176.74.176.148 to version by Myoglobin. Report False Positive? Thanks, ...
Myoglobin. (talk , contribs)‎ (→‎Diagnostic criteria: ce) (Tag: 2017 source edit). *(diff , hist) . . m Dental plaque‎; 09:09 ...
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- ...
"Activation Energy Spectrum in Myoglobin---a Comment". Physical Review Letters. 34 (13): 845. Bibcode:1975PhRvL..34..845A. doi: ...
... because they bond to the myoglobin and act as a substitute for the oxygen, thus turning myoglobin red. More recent evidence ... 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 ...
... 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 ...
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 ...
It has a high affinity for myoglobin, about 60 times greater than that of oxygen. Carbon monoxide bound to myoglobin may impair ... Additionally, myoglobin and mitochondrial cytochrome oxidase are affected. Diagnosis is based on a HbCO level of more than 3% ... 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 ...
... some deaths have been reported due to the release of myoglobin from ruptured muscle cells. High amounts of myoglobin can induce ...
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 ...
About 4% is bound up in myoglobin molecules. Around 30% of the iron in the body is stored as ferritin or hemosiderin in the ...
Moreover, myoglobin has the highest affinity to oxygen. Differences between myoglobin (Mb), fetal hemoglobin (Hb F), adult ... In contrast, 2,3-BPG has no effect on the related compound myoglobin.(reference required) In pregnant women, there is a 30% ...
The muscle pigment, myoglobin, provides an effective bond. This additional oxygen storage is vital for deep diving, since ...
... 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: ...
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 ...
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 ...
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. ...
Callaway, David J. E. (1994). "Solvent-induced organization: a physical model of folding myoglobin". Proteins: Structure, ...
Callaway, David J. E. (1994). "Solvent-induced organization: a physical model of folding myoglobin". Proteins: Structure, ...
... tissue contains less myoglobin than fully aquatic mammals. When diving, their heart rate decreases to 60 beats per ... "Evolution of Mammalian Diving Capacity Traced by Myoglobin Net Surface Charge". Science. 340 (6138). doi:10.1126/science. ...
They both make use of the high affinity of hemoglobin and myoglobin for the gas. Carbon monoxide also combines with hemoglobin ... Carbon monoxide has a dissociation velocity which is 100 times less than that of oxygen; its affinity for myoglobin is 40 times ... 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 ...
Other oxygen transport systems include myoglobin, hemocyanin, and hemerythrin. Oxidases and oxygenases are metal systems found ...
Myoglobin contains 153 amino acids.[27] Myoglobin contains a porphyrin ring with an iron at its center. A proximal histidine ... In humans, myoglobin is encoded by the MB gene.[18] Myoglobin can take the forms oxymyoglobin (MbO2), carboxymyoglobin (MbCO), ... Myoglobin serves both as an O2 buffer and to store O2 in muscle. All known vertebrate myoglobins and β-hemoglobin subunits are ... Myoglobin is released from damaged muscle tissue (rhabdomyolysis), which has very high concentrations of myoglobin.[23] The ...
Mb; Myoglobin; PVALB (Parvalbumin) Myoglobin (Mb) is a monomeric, cytoplasmic hemoprotein with rich and varied history, thus ... Myoglobin (Mb) is a monomeric, cytoplasmic hemoprotein with rich and varied history, thus becoming an object of renewed ... Swain N., Patel S., Hosalkar R.M. (2018) Myoglobin (Mb). In: Choi S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham ...
Myoglobin, a protein found in the muscle cells of animals. It functions as an oxygen-storage unit, providing oxygen to the ... mammals such as seals and whales are able to remain submerged for long periods because they have greater amounts of myoglobin ... meat are related to the myoglobin content of muscle fibres and to the chemical state of the iron atom found in the myoglobin ... muscles contain a respiratory pigment, myoglobin. There are relatively few myoglobin-containing cells in "white meat," whereas ...
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 ...
What does the myoglobin do? Myoglobin are the oxygen carrying pigment in muscles of humans and other mammals. Myoglobin ... What is Myoglobins? Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and ... What is the role of the Myoglobin? Myoglobin is a monomeric heme protein found mainly in muscle tissue where it serves as an ... What is the role of Myoglobin? Myoglobin is a protein found in muscle tissue of vertebrates that is iron- and oxygen-binding. ...
Urine Myoglobin; Serum Myoglobin Formal name:. Myoglobin Related tests:. CK, CK-MB, Troponin, Cardiac Biomarkers All content on ... Should everyone with muscle pain and weakness have a myoglobin test?. General, routine testing for myoglobin is usually not ... Myoglobin is filtered from the blood by the kidneys and is released into the urine. Large quantities of myoglobin are toxic to ... A myoglobin blood test may be used detect muscle damage. Myoglobin is a small, oxygen-binding protein found in heart and ...
Myoglobin definition, hemoglobin of muscle, weighing less and carrying more oxygen and less carbon monoxide than blood ... myoglobin. myofibrositis, myofilament, myogenesis, myogenic, myogenous, myoglobin, myoglobinuria, myoglobulin, myoglobulinuria ... Myoglobin combines with oxygen released by red blood cells and transfers it to the mitochondria of muscle cells, where it is ...
Hypoxia-inducible myoglobin expression in nonmuscle tissues. Jane Fraser, Luciane Vieira de Mello, Deborah Ward, Huw H. Rees, ... Hypoxia-inducible myoglobin expression in nonmuscle tissues. Jane Fraser, Luciane Vieira de Mello, Deborah Ward, Huw H. Rees, ... Hypoxia-inducible myoglobin expression in nonmuscle tissues. Jane Fraser, Luciane Vieira de Mello, Deborah Ward, Huw H. Rees, ... Myoglobin (Myg) has been intensively studied for many years in relation to protein structure (1). Myg is widely thought to be ...
I was wondering today whether it would be possible to isolate myoglobin from the blood of a deep diving sea mammal, and ... Its actually not in the myoglobin, Dr. Satan, your evil-ness. Its all in the ability to regulate your metabolism and how your ... I was wondering today whether it would be possible to isolate myoglobin from the blood of a deep diving sea mammal, and ...
Myoglobin contains 154 amino acids.[19]. Myoglobin contains a porphyrin ring with an iron at its center. A proximal histidine ... In humans myoglobin is encoded by the MB gene.[12]. Myoglobin can take the forms oxymyoglobin (MbO2), carboxymyoglobin (MbCO), ... Myoglobin is the primary oxygen-carrying pigment of muscle tissues.[7] High concentrations of myoglobin in muscle cells allow ... Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin.[6] Myoglobin is found in ...
Ligand pathways in myoglobin: A review of trp cavity mutations.. Olson, J.S., Soman, J., Phillips, G.N.. (2007) IUBMB Life 59: ... The pathways for ligand entry and exit in myoglobin have now been well established by a wide variety of experimental results, ... The pathways for ligand entry and exit in myoglobin have now been well established by a wide variety of experimental results, ... mechanism in which ligands move into and out of myoglobin by outward rotation of the HisE7 side chain, but after entry can ...
Myoglobin (Mb) has for many years played the role of such a prototype. It appears to be simple enough so that many of its ...
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The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Myoglobin is inefficiently removed by dialysis, and can lead to kidney failure, significantly increasing the risk of death. ... CytoSorb® Adds Bilirubin and Myoglobin Reduction to European Union Approved Indications for Use. News provided by ... CytoSorb® Adds Bilirubin and Myoglobin Reduction to European Union Approved Indications for Use Broadened indications expand ... One life-threatening complication in severe trauma is excessive myoglobin release, or rhabdomyolysis, due to the destruction of ...
Myoglobin. P02144. Details. Drug Relations. Drug Relations. DrugBank ID. Name. Drug group. Pharmacological action?. Actions. ... Myoglobin. Kind. protein. Organism. Humans. Protein. Name. UniProt ID. ...
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The diffusion path for myoglobin is tortuous, the local concentration of myoglobin may be great, and myoglobin-facilitated ... myoglobin messenger RNA is elevated under conditions eliciting myoglobin formation (Williams and Neufer, 1996). Myoglobin is ... Myoglobin. Myoglobin is a relatively small protein (Mr 17 600) that is little affected by environmental conditions [with the ... Mice without myoglobin. Knockout of the myoglobin-encoding gene (Garry et al., 1998; Godecke et al., 1999) induces multiple ...
Myoglobin is a protein that is able to bind oxygen. Myoglobin, which is similar to haemoglobin, is the main oxygen-carrying ... Ordway G.A. & Garry D.J. (2004). "Myoglobin: an essential hemoprotein in striated muscle". J. Exp. Biol. 207 (Pt 20): 3441-6. ... In humans, increased level of myoglobin in the serum of the blood can be an indication of myocardial infarction. Other factors ... Seals and other marine mammals have more myoglobin in their muscles than land animals. ...
Since CO rebinds to myoglobin within a few milliseconds, the pump-probe sequence could be repeated on a single myoglobin ... The mutant L29F of myoglobin [1], in which a leucine residue is replaced by a phenylalanin, proved to be an interesting test ... The system studied by this team, the oxygen storage protein myoglobin, is similar to hemoglobin but is found in muscle cells ... configuration helps drive CO out of its primary docking site on a timescale a thousand-fold faster than in wild-type myoglobin ...
Determination of the redox state of myoglobin (Mb) gives useful information for evaluating the quality of tuna meat. To attain ... An example of a myoglobin lacking the D helix. Acta Cryst D 50:283-289CrossRefGoogle Scholar ... Myoglobin Streamlined isolation Preparative electrophoresis Autoxidation Tuna Electronic supplementary material. The online ... Chen WL, Chow CJ (2001) Studies on the physicochemical properties of milkfish myoglobin. J Food Biochem 25:157-174CrossRef ...
... which means they require a lot of myoglobin. Until the gift of the sperm whale meat, Kendrew couldnt isolate enough myoglobin ... Myoglobin Protein Model a" data-cycle-caption="#nmah-edan-caption" data-cycle-auto-height="container" data-cycle-caption- ... Myoglobins purpose in the body is to store oxygen in the muscles until needed. Sperm whales, as aquatic mammals, have to be ... Interestingly, Kendrew had a hard time getting enough crystals of myoglobin to work with until someone was kind enough to give ...
We report here a neutron structure of fully deuterated sperm whale myoglobin (Mb), by using a single crystal and data to 2.0-Å ... Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin. Fong Shu, Venki Ramakrishnan, ... Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin ... Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin ...
Montse Olivé have described in Nature Communications a new muscular disease caused by a mutation in the myoglobin gene. ... Myoglobin, the protein that gives muscles their red color, has as its main function the transportation and intracellular ... This is the first time that a disease caused by a mutation in the myoglobin gene has been identified, says Montse Olivé, ... Montse Olivé have described in Nature Communications a new muscular disease caused by a mutation in the myoglobin gene. The ...
Myoglobin Calibrator. Dedicated Myoglobin calibrator designed specifically for use with immunoturbidimetric Myoglobin assays. ... Tags: Randox Biosciences, Research, Immunology, Myoglobin, cardiac, cytokine, troponin, Molecular, Oncology, metabolic syndrome ... Tags: Randox Biosciences, Research, Immunology, Myoglobin, cardiac, cytokine, troponin, Molecular, Oncology, metabolic syndrome ...
タンパク質ミオグロビンのボゾンピークおよびフラクトンダイナミクス研究 [in Japanese] Boson peak and fracton of protein myoglobin [in Japanese] * * 泉二 玲緒奈
Urine myoglobin; Heart attack - myoglobin urine test; Myositis - myoglobin urine test; Rhabdomyolysis - myoglobin urine test ... Myoglobin urine test. Definition. The myoglobin urine test is done to detect the presence of myoglobin in urine. ... 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 ...
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Myoglobin can be checked with a blood test or a urine test. Levels in the blood will increase within about 3... ... Myoglobin is a protein found in heart tissue and other muscles. It is released into the blood after damage to the heart or ... Myoglobin. Test Overview. Myoglobin is a protein found in heart tissue and other muscles. It is released into the blood after ... The myoglobin test is used to look for disease or injury of muscle tissue. The urine test can help check for rhabdomyolysis. ...
  • 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 to the body through the muscles and blood. (petmd.com)
  • Unlike hemoglobin and myoglobin, iron-bound Lf is reasonably stable to gastric and duodenal digestive conditions. (wellnessresources.com)
  • The transfer of heme iron from either intact or digested forms of hemoglobin and myoglobin and from intact ferritin was demonstrated by in vitro methods, monitoring Fe-saturation status of Lf by changes in absorptivity at 465 nm. (wellnessresources.com)
  • Compare and contrast hemoglobin and myoglobin. (coursehero.com)
  • Myoglobin is released from damaged muscle tissue ( rhabdomyolysis ), which has very high concentrations of myoglobin. (wikipedia.org)
  • Sometimes, a urine test is ordered to evaluate myoglobin levels in people who have had extensive damage to their skeletal muscles (rhabdomyolysis). (labcorp.com)
  • A significantly elevated level of myoglobin may be caused by rhabdomyolysis . (labcorp.com)
  • One life-threatening complication in severe trauma is excessive myoglobin release, or rhabdomyolysis, due to the destruction of muscle tissue. (prnewswire.com)
  • 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)
  • Lappalainen H. Elimination kinetics of myoglobin and creatine kinase in rhabdomyolysis: implications for follow-up. (medigraphic.com)
  • Rodr guez-Capote K, Balion CM, Hill SA, Cleve R, Yang L, El Sharif A. Utility of urine myoglobin for the prediction of acute renal failure in patients with suspected rhabdomyolysis: a systematic review. (medigraphic.com)
  • We have found haem-protein cross-linked myoglobin in the urine of patients suffering from rhabdomyolysis and haem-protein cross-linked haemoglobin in the cerebrospinal fluid of patients following subarachnoid haemorrhage. (biochemsoctrans.org)
  • We have previously proposed that these oxidation processes in rhabdomyolysis include the formation of potent vasoconstrictor molecules, generated by the myoglobin-catalysed oxidation of membranes, inducing nephrotoxicity and renal failure. (biochemsoctrans.org)
  • What is the role of Myoglobin? (answers.com)
  • 1.Garry, D. J. and Memmen, P. P. A. (2007) Molecular insights into the functional role of myoglobin. (leebio.com)
  • The physiological role of myoglobin depends on the modulation of heme activity by the protein. (rice.edu)
  • The role of myoglobin in dioxygen binding in cardiomyocytes and oxidative skeletal muscle has widely been appreciated. (visualsonics.com)
  • Our results reveal a physiological role of myoglobin in FA metabolism with the lipid accumulation- suppressing effects of myoglobin preventing cardiac lipotoxicity. (visualsonics.com)
  • The potential role of myoglobin spin and redox states in initiating lipid oxidation is reviewed. (dtu.dk)
  • Western Blot: Myoglobin Antibody (SC06-38) [NBP2-67599] - Analysis of Myoglobin on human skeletal muscle lysates using anti-Myoglobin antibody at 1/1,000 dilution. (novusbio.com)
  • Immunohistochemistry-Paraffin: Myoglobin Antibody (SC06-38) [NBP2-67599] - Analysis of paraffin-embedded mouse skeletal muscle tissue using anti-Myoglobin antibody. (novusbio.com)
  • In order to determine if this increase is due to myocardial damage, the right ventricle of 24 naturally infected dogs was examined by routine histology and immunohistochemistry with anti-myoglobin and anti-cardiac troponin I antibodies. (biomedsearch.com)
  • [16] 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. (wikipedia.org)
  • Myoglobin belongs to the globin superfamily of proteins, and as with other globins, consists of eight alpha helices connected by loops. (wikipedia.org)
  • Muscle damage releases myoglobin into the blood plasma, but it does not bind to serum proteins. (petmd.com)
  • 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)
  • Together, these two proteins show how protein structure determines function and how Nature uses components, in this case myoglobin, to build more complex proteins consisting of functional subunits. (springer.com)
  • Myoglobin is a part of the globin superfamily of proteins, consisting of eight alpha helices connected by loops, with a total content of 154 amino acids and a molecular weight of 17.7 kDa 1, 2, 4 . (leebio.com)
  • Lactoferrin (Lf), present in colostrum and milk is a member of the transferrin family of iron-binding glyco-proteins, with stronger binding capacity to ferric iron than hemoglobin, myoglobin or transferrin. (wellnessresources.com)
  • Furthermore, by applying the model into two well studied real proteins (myoglobin and villin headpiece HP35), it is shown that the multi-kink model gives correct folding pathway and thermal dynamical properties compared with the experimental results for both proteins. (diva-portal.org)
  • Cobalt(III)-induced unfolding of myoglobin is unique in its selectivity (other proteins are unaffected) and in allowing the isolation of the partially folded macromolecule (the protein does not refold or aggregate upon removal of free denaturant). (caltech.edu)
  • When the level of myoglobin is too high, it can damage the kidneys. (medlineplus.gov)
  • The level of myoglobin in the blood starts to rise within 2-3 hours of a heart attack or other muscle injury, reaches its highest levels within 8-12 hours, and generally falls back to normal within one day. (labcorp.com)
  • In humans, increased level of myoglobin in the serum of the blood can be an indication of myocardial infarction . (wikipedia.org)
  • 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. (acpjc.org)
  • Blood levels of myoglobin can rise very quickly with severe muscle damage and can be measured within a few hours following an injury. (labcorp.com)
  • Myoglobin excretion was correlated to excretion of beta 2-microglobulin (P less than 0.02) but not to serum levels of myoglobin. (nih.gov)
  • What can cause high blood levels of myoglobin other than damage to skeletal muscle or heart muscle? (healthtap.com)
  • After muscle tissue damage such as crush injuries, burns, myocardial infarction and muscle diseases, increased levels of myoglobin are found in the blood and urine. (perkinelmer.com)
  • It has recently been reported that dogs affected by canine heartworm disease (Dirofilaria immitis) can show an increase in plasma levels of myoglobin and cardiac troponin I, two markers of muscle/myocardial injury. (biomedsearch.com)
  • Results confirm that increased levels of myoglobin and cardiac troponin I are indicative of myocardial damage in dogs affected by heartworm disease. (biomedsearch.com)
  • In 1962 a share of the Nobel Prize for Chemistry was awarded to John C. Kendrew for work, utilizing the technique of X-ray diffraction , that permitted construction of a three-dimensional model of crystalline sperm-whale myoglobin. (britannica.com)
  • Professor Jonathan Wittenberg used this model of sperm whale myoglobin structure as a teaching tool at the Albert Einstein College of Medicine at Yeshiva University in the Bronx. (si.edu)
  • Interestingly, Kendrew had a hard time getting enough crystals of myoglobin to work with until someone was kind enough to give him a slab of sperm whale meat. (si.edu)
  • Until the gift of the sperm whale meat, Kendrew couldn't isolate enough myoglobin to grow crystals of sufficient size for his research. (si.edu)
  • We report here a neutron structure of fully deuterated sperm whale myoglobin (Mb), by using a single crystal and data to 2.0-Å resolution. (pnas.org)
  • Sperm whale myoglobin was chosen as a simple model system for determining the structural and chemical factors that regulate NO reactivity. (rice.edu)
  • Molecular analysis of a heteroclitic T cell response to the immunodominant epitope of sperm whale myoglobin. (jimmunol.org)
  • We have investigated the molecular basis for binding and Ag presentation of an immunodominant Th cell determinant of sperm whale myoglobin, a prototype amphipathic helical structure in the native protein. (jimmunol.org)
  • 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 ). (biochemj.org)
  • Here, we describe myoglobin-augmented oxygen supply to heart and red muscle, taking into account their three-dimensional structures and the elevated concentration of myoglobin in the cytoplasmic domain to which it is restricted and recognizing the large area of mitochondrial surface available for oxygen diffusion. (biologists.org)
  • The mean serum concentration of myoglobin in ninety-nine healthy blood donors was 44.3 microgram/l +/- 18.0 microgram/l (SD) with a significant difference (P less than 0.001) between men (50.6 +/- 19.8) and women (35.7 +/- 10.4). (nih.gov)
  • The amount of oxygen bound to myoglobin is a function of the oxygen concentration and the affinity of myoglobin for oxygen. (coursehero.com)
  • Wehn the initial sample was drawn between 12 and 24 h after admission in another group of 20 patients with acute myocardial infarcts, the mean serum myoglobin concentration was 195+/-47 ng/ml, and 11 of these individuals had normal levels. (jci.org)
  • The serum concentration of myoglobin in 21 additional patients admitted with chest pain but without acute myocardial infarction was 41+/-6 ng/ml. (jci.org)
  • Because the concentration of myoglobin in cardiac and red skeletal muscle is very great, reaching 3 mmol l -1 in the sarcoplasmic domain to which it is confined, it is not surprising that myoglobin serves multiple functions. (biologists.org)
  • Development of myoglobin concentration and acid buffering capacity in harp (Pagophilus groenlandicus) and hooded (Cystophora cristata) seals from b. (nih.gov)
  • Development of myoglobin concentration and acid buffering capacity in harp (Pagophilus groenlandicus) and hooded (Cystophora cristata) seals from birth to maturity. (nih.gov)
  • To investigate the pattern of muscle development, myoglobin concentration ([Mb]) and acid buffering ability (beta) was measured in ten muscles from 23 harp and 40 hooded seals of various ages. (nih.gov)
  • Oxy-, deoxy-, and met-myoglobin concentration changes over storage time were also calculated using Beer-Lamberts' law with reflectance intensities at 557, 582, and 630 nm. (spiedigitallibrary.org)
  • The Myoglobin was isolated by cation-exchange chromatography, and concentration of Myoglobin is measured by spectrophotometry. (ukessays.com)
  • The concentration of the purified Myoglobin was determined to be 0.072 ug/uL. (ukessays.com)
  • Serum concentration of myoglobin increases above the normal range as early as 1 hour after myocardial infarction, and peak in approximately 4 to 8 hours after onset. (rapidtest.com)
  • The net surface charge of the oxygen-storing muscle protein myoglobin ( Z Mb ), which can be readily determined from its primary structure, provides an objective target to address this question due to mechanistic linkages with myoglobin concentration. (elifesciences.org)
  • Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. (wikipedia.org)
  • Diving mammals such as seals and whales are able to remain submerged for long periods because they have greater amounts of myoglobin in their muscles than other animals do. (britannica.com)
  • Myoglobin is a protein in heart and skeletal muscles. (medlineplus.gov)
  • 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 are the oxygen carrying pigment in muscles of humans and other mammals. (answers.com)
  • Myoglobin comprise a combination of protein and iron and are the cause of the red color … of muscles in the skeleton. (answers.com)
  • In animals, diving mammals like seals or whales posses muscles with high abundance of myoglobin because it is the principle oxygen carrying pigment of muscle tissues and high concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. (answers.com)
  • Seals and other marine mammals have more myoglobin in their muscles than land animals. (wikipedia.org)
  • Sperm whales, as aquatic mammals, have to be very efficient at storing oxygen for their muscles during deep sea dives, which means they require a lot of myoglobin. (si.edu)
  • Myoglobin, the protein that gives muscles their red color, has as its main function the transportation and intracellular storage of oxygen, acting as an oxygen reservoir when there are low levels (hypoxia) or a total lack thereof (anoxia). (news-medical.net)
  • Finally, researchers from the universities of Modena and Vienna have identified an alteration in the biochemical and thermodynamic properties of the mutated myoglobin, including an alteration in the oxygen-binding capacity that contributes to the formation of the lipid and protein aggregates that are found in the muscles of the patients. (news-medical.net)
  • Myoglobin is a protein found in heart tissue and other muscles. (peacehealth.org)
  • Myoglobin is a protein found in muscles. (peacehealth.org)
  • 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)
  • Increasing the number of charged amino acids allows for higher myoglobin concentrations in the muscles of diving mammals. (sciencemag.org)
  • The heart, red skeletal muscles and the nitrogen-fixing legume root nodule function in steady states of high oxygen influx, partial oxygenation of cytoplasmic myoglobin or leghemoglobin and correspondingly low oxygen partial pressure. (biologists.org)
  • Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. (prospecbio.com)
  • Myoglobin is an iron- and oxygen-binding protein, serving as a reserve oxygen supply and facilitating oxygen transport in muscles. (leebio.com)
  • Myoglobin is small protein found in skeletal muscles and the heart, which binds oxygen. (transparencymarketresearch.com)
  • Abstract The dynamics of selected conformational coordinates, key roles in the understanding of the CO-rebinding process, are investigated in horse heart carbonmonoxy myoglobin (MbCO) through time-resolved X-ray absorption spectroscopy. (ebscohost.com)
  • Like hemoglobin, myoglobin is a cytoplasmic protein that binds oxygen on a heme group. (wikipedia.org)
  • Myoglobin (Mb) is a monomeric, cytoplasmic hemoprotein with rich and varied history, thus becoming an object of renewed interest owing to its role beyond those previously described. (springer.com)
  • Myoglobin is a low molecular weight, cytoplasmic serum protein. (rapidtest.com)
  • The AlphaLISA ® Human Myoglobin Detection Kit is designed for detection and quantitation of human myoglobin in serum, buffered solution or cell culture medium in a homogeneous (no-wash steps, no separation steps) assay. (perkinelmer.com)
  • [23] The released myoglobin is filtered by the kidneys but is toxic to the renal tubular epithelium and so may cause acute kidney injury . (wikipedia.org)
  • The kidneys help remove myoglobin from the blood into the urine. (medlineplus.gov)
  • Myoglobin is filtered from the blood by the kidneys and is released into the urine. (labcorp.com)
  • Urine myoglobin levels reflect the degree of muscle injury and, since myoglobin is toxic to the kidneys, reflect the risk of kidney damage. (labcorp.com)
  • Urine myoglobin may be ordered when there has been extensive injury to skeletal muscle, resulting in the rapid breakdown of muscle, and damage to the kidneys is suspected. (labcorp.com)
  • Consequently, plasma color does not change, and the myoglobin is quickly cleared from the blood by the liver and kidneys. (petmd.com)
  • Your kidneys filter your blood for myoglobin so that it can be passed out of your body in your urine. (ahealthyme.com)
  • But too much myoglobin can overwhelm your kidneys and lead to kidney failure. (ahealthyme.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 released from damaged muscle tissue into the bloodstream and is filtered by the kidneys, potentially causing acute kidney injury. (leebio.com)
  • Excessive quantity of myoglobin is toxic to the kidneys. (transparencymarketresearch.com)
  • Finally, we report the 0.95-A structure of ferrous nitrosyl myoglobin, which provides an accurate structural view of the NO coordination geometry in the context of a globin heme pocket. (rcsb.org)
  • 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. (osti.gov)
  • Once O 2 is bound to the myoglobin, a structural change occurs to the iron center as the iron is oxidized to an oxidation state of 3+. (leebio.com)
  • UVPD provided insight into the stability of native structural elements of holo-myoglobin. (rsc.org)
  • In all mutants, structural perturbations are limited to the site of the substitution and the flexible corner regions of myoglobin. (rice.edu)
  • Using site-directed mutagenesis, the amino acids Leu89, Ser92, and His97 have been changed to understand why these residues are highly conserved in myoglobin across species, to elucidate the structural and functional roles played by these residues. (illinois.edu)
  • In this thesis, we have explored the possibility of using 4-fluorotryptophan as an electrostatic probe in myoglobin and hemoglobin to gain both electrostatic and structural information via $\sp{19}$F-NMR. (illinois.edu)
  • High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. (wikipedia.org)
  • Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. (prospecbio.com)
  • Serum myoglobin was positively correlated to age (P less than 0.05), body weight (P less than 0.02), serum creatine kinase (P less than 0.001), and serum creatinine (P less than 0.001) to galactose elimination rate. (nih.gov)
  • Myoglobin and creatine kinase in acute myocardial infarction. (bmj.com)
  • To compare the predictive capacity of myoglobin, total creatine kinase and urine hemoglobin for acute renal injury in patients with trauma. (medigraphic.com)
  • Myoglobin, total creatine kinase, creatinine and hemoglobin levels were measured in urine at their admission. (medigraphic.com)
  • Levels of total creatine kinase and myoglobin did not prove to be adequate predictors of kidney injury because there was no significant difference. (medigraphic.com)
  • Can creatine kinase-MB (CKMB), cardiac troponin T (troponin), and myoglobin levels identify failed reperfusion after intravenous thrombolytic therapy in acute myocardial infarction (MI)? (acpjc.org)
  • In patients with acute myocardial infarction, changes in the levels of creatine kinase-MB, cardiac troponin T, and myoglobin for periods of 60 and 90 minutes identified failed reperfusion. (acpjc.org)
  • [25] However, elevated myoglobin has low specificity for acute myocardial infarction (AMI) and thus CK-MB , cardiac troponin , ECG , and clinical signs should be taken into account to make the diagnosis. (wikipedia.org)
  • A radioimmunoassay has been developed for the measurement of serum myoglobin in order to evaluate the time-course and frequency of myoglobinemia in patients with acute myocardial infarction. (jci.org)
  • Radioimmunoassay of serum myoglobin appears to be useful and sensitive test for the early detection of myocardial infarction. (jci.org)
  • This 3 in 1 Cardiac Markers Rapid Test is designed for qualitative determination of cardiac Troponin I, CK-MB, and Myoglobin in human serum specimen as an aid in the diagnosis of myocardial infarction. (rapidtest.com)
  • No indications of circulating antibodies to myoglobin were obtained when assaying sixty-seven rheumatoid arthritis and thirteen myastenia gravis sera. (nih.gov)
  • 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)
  • Based on the modeled structures of the mutants using CHARMM, and the evidence presented in this thesis, we propose that not only is the orientation of the proximal histidine important in controlling ligand binding to the heme, the dynamics of the F-helix also play an important role in controlling the inner barrier in myoglobin and hemoglobin. (illinois.edu)
  • Ultrafast protein dynamics of the CO adduct of a myoglobin mutant with the polar distal histidine replaced by a nonpolar valine (H64V) have been investigated by spectrally resolved infrared stimulated vibrational echo experiments and molecular dynamics (MD) simulations. (nih.gov)
  • Myoglobin is a monomeric heme protein found mainly in muscle tissue where it serves as an intracellular storage site for oxygen. (answers.com)
  • Myoglobin (Mb), an oxygen-binding heme protein highly expressed in heart and skeletal muscle, has been shown to undergo oxidative modifications on both an inter- and intramolecular level when exposed to hydrogen peroxide (H 2 O 2 ) in vitro. (mdpi.com)
  • Myoglobin is a heme protein with a molecular weight of approximately 17.5 kDa. (perkinelmer.com)
  • Myoglobin can also be measured with a urine test . (medlineplus.gov)
  • The myoglobin urine test is done to detect the presence of myoglobin in urine. (floridahealthfinder.gov)
  • Myoglobin can be checked with a blood test or a urine test. (peacehealth.org)
  • In some cases, healthcare providers will use a urine test for myoglobin to help find the hazard and protect your kidney health. (ahealthyme.com)
  • Myoglobin (symbol Mb or MB ) is an iron - and oxygen -binding protein found in the skeletal muscle tissue of vertebrates in general and in almost all mammals. (wikipedia.org)
  • Myoglobin is a protein found in muscle tissue of vertebrates that is iron- and oxygen-binding. (answers.com)
  • Myoglobin does help to transport oxygen in oxidative muscle tissue, but does not directly play a role in contraction. (answers.com)
  • An increase in blood myoglobin means that there has been very recent injury to muscle tissue. (labcorp.com)
  • The myoglobin test is used to look for disease or injury of muscle tissue. (peacehealth.org)
  • Myoglobin is a protein found in muscle tissue, where it binds to and stores oxygen to be used during strenuous exercise. (sciencephoto.com)
  • Myoglobin, a protein in muscle tissue that stores oxygen, is what gives meat its red pigment. (phys.org)
  • The colour that meat takes is partly determined by the degree of oxidation of the myoglobin. (wikipedia.org)
  • Faustman C, Sun Q, Mancini R, Suman SP (2010) Myoglobin and lipid oxidation interactions: mechanistic bases and control. (springer.com)
  • We here unravel a novel role of cardiac myoglobin in governing FA metabolism to ensure the physiological energy production through β-oxidation, preventing myocardial lipid accumulation and preserving cardiac functions. (visualsonics.com)
  • An overview of myoglobin-initiated lipid oxidation in simple model systems, muscle, and muscle-based foods is presented. (dtu.dk)
  • Andersen, H.J. / Myoglobin-induced lipid oxidation : A review . (dtu.dk)
  • We used femtosecond infrared polarization spectroscopy and density functional theory in a study on the key signaling molecule nitric oxide (NO) bound to myoglobin. (fu-berlin.de)
  • The function of myoglobin is to? (answers.com)
  • The principal function of myoglobin is to transport oxygen from the sarcolemma to the mitochondria in heart and muscle cells. (perkinelmer.com)
  • Birnbaum GI, Evans SV, Przybylska M, Rose DR (1994) 1.70 Å resolution structure of myoglobin from yellowfin tuna. (springer.com)
  • Kendrew uncovered the structure of myoglobin using a method known as X-ray crystallography, a technique where crystals of a substance-in this case myoglobin-are grown and then bombarded with X-rays. (si.edu)
  • We develop a highly predictive energy function to describe the low temperature crystallographic structure of myoglobin with sub-\AA ngstr\"om precision. (diva-portal.org)
  • Two solid-phase radioimmunoassays have been developed for the detection of myoglobin in serum and urine. (nih.gov)
  • In this work, a novel electrochemical aptasensor was developed for sensitive and selective detection of myoglobin based on meso-tetra (4-carboxyphenyl) porphyrin-functionalized graphene-conjugated gold nanoparticles (TCPP-Gr/AuNPs). (mdpi.com)
  • Due to its good electric conductivity, large specific surface area, and excellent mechanical properties, TCPP-Gr/AuNPs can act as an enhanced material for the electrochemical detection of myoglobin. (mdpi.com)
  • Sometimes, a myoglobin blood test may be used along with a troponin test as a cardiac biomarker to help detect a heart attack early, but in the U.S., it is used less frequently for this purpose. (labcorp.com)
  • An increase in myoglobin is detectable sooner than troponin, but it is not as specific for heart damage and it will not stay elevated as long as troponin. (labcorp.com)
  • Although a negative myoglobin result effectively rules out a heart attack, a positive result must be confirmed by testing for troponin. (labcorp.com)
  • Myoglobin is not widely used for diagnosing heart attacks because it has largely been replaced by Troponin, which is much more specific. (labcorp.com)
  • When used as a cardiac biomarker , an increase in blood myoglobin may mean that a heart attack has occurred recently but because myoglobin is also found in skeletal muscle, a troponin test is required for confirmation. (labcorp.com)
  • These five areas include our Metabolic Syndrome Array 1 & 2, Cytokine Arrays and Cardiac Array including CK-MB, H-FABP, Myoglobin and Troponin. (randox.com)
  • Myocardial damage in dogs affected by heartworm disease (Dirofilaria immitis): Immunohistochemical study of cardiac myoglobin and troponin I in naturally infected dogs. (biomedsearch.com)
  • Diagnostic Automation/Cortez Diagnostics Inc. offers a 3 in 1 Troponin I/Myoglobin/CK-MB Serum Rapid Test (Cassette) RapiCard Insta Test which is an immunochromatography-based one-step in vitro test for diagnostic. (rapidtest.com)
  • Diagnostic Automation Inc. offers an additional 3 in 1 Cardiac Marker Rapid Test-the Troponin I/Myoglobin/CK-MB Rapid Test for Serum/Whole Blood specimen. (rapidtest.com)
  • Blood samples drawn before thrombolytic therapy and at 30, 60, 90, and 120 minutes were analyzed for levels of CKMB, troponin, and myoglobin. (acpjc.org)
  • 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. (acpjc.org)
  • Myoglobin , a protein found in the muscle cells of animals. (britannica.com)
  • Myoglobin is a small, oxygen-binding protein found in heart and skeletal muscle. (labcorp.com)
  • Dynamics of ligand binding to myoglobin. (nih.gov)
  • Furthermore, residues number 87 to 94 have been replaced by the amino acids in the respective locations in hemoglobin $\beta$-chain (residues number 86 to 93) to examine the importance of the F-helix in controlling ligand binding in myoglobin and hemoglobin $\beta$-chain. (illinois.edu)
  • There is a close chemical similarity between myoglobin and hemoglobin , the oxygen-binding protein of red blood cells. (britannica.com)
  • Compared to hemoglobin , myoglobin has a higher affinity for oxygen and does not have cooperative-binding with oxygen like hemoglobin does. (wikipedia.org)
  • Likewise, leghemoglobin, a protein similar to myoglobin but with 10-fold greater oxygen affinity, transports oxygen from the cell membrane of the central cells of the legume root nodule to the symbiosomes, which are membrane-bound intracellular organelles housing the bacteroids, the intracellular nitrogenfixing form of the bacterium Rhizobium ( Appleby, 1984 ). (biologists.org)
  • Myoglobin has a six times higher affinity to bind oxygen than hemoglobin. (doccheck.com)
  • Myoglobin has a strong affinity for oxygen when it is in the lungs, and where the pressure is around 100 torr. (wikibooks.org)
  • This makes myoglobin less efficient of an oxygen transporter than hemoglobin, which loses it's affinity for oxygen as the pressure goes down and releases the oxygen into the tissues. (wikibooks.org)
  • Myoglobin (Myg) is an oxygen-binding hemoprotein that is widely thought to be expressed exclusively in oxidative skeletal and cardiac myocytes, where it plays a key role in coping with chronic hypoxia. (pnas.org)
  • Myoglobin is expressed in cardiac myocytes and oxidative skeletal muscle fibres. (perkinelmer.com)
  • Haem-protein cross-linked myoglobin and haemoglobin are generated by ferric-ferryl redox cycling, and thus can be used as markers of oxidative stress. (biochemsoctrans.org)
  • 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. (osti.gov)
  • The hyperbolic binding curve is characteristic for myoglobin and distinguishes myoglobin from hemoglobin which has a sigmoidal binding curve. (doccheck.com)
  • Immunocytochemistry/ Immunofluorescence: Myoglobin Antibody (SC06-38) [NBP2-67599] - Staining Myoglobin in C2C12 cells (green). (novusbio.com)
  • Swain N., Patel S., Hosalkar R.M. (2018) Myoglobin (Mb). (springer.com)
  • Myoglobin (CAS 9008-45-1) Market Research Report 2018 aims at providing comprehensive data on myoglobin market globally and regionally (Europe, Asia, North America, Latin America etc. (marketpublishers.com)
  • Myoglobin (CAS 9008-45-1) Market Research Report 2018 contents were prepared and placed on the website in March, 2018. (marketpublishers.com)
  • Please note that Myoglobin (CAS 9008-45-1) Market Research Report 2018 is a half ready publication and contents are subject to change. (marketpublishers.com)
  • Myoglobin is a globular protein and consists of eight α-helixes in its secondary structure. (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)
  • Myoglobin is an oxygen-binding globular protein which is vital in facilitating the acquisition and utilization of oxygen in animals. (ukessays.com)
  • Myoglobin is a globular protein which contains a single polypeptide chain of about 153 amino acids and an iron-porphyrin complex, or the heme group (3). (ukessays.com)
  • Pigeon heart mitochondria were isolated with minimal damage to the outer mitochondrial membrane and were incubated at low oxygen pressures, where respiration is oxygen limited, with solutions of each of six monomeric hemoglobins with widely divergent kinetics and equilibria in their reactions with oxygen: Busycon myoglobin, horse myoglobin, Lucina hemoglobins I and II, soybean leghemoglobin c and Gasterophilus hemoglobin. (biologists.org)
  • The oxygen binding curve for Myoglobin forms an asymptotic shape, which shows a simple graph that rises sharply then levels off as it reaches the maximum saturation. (wikibooks.org)
  • The half-saturation, the point at which half of the myoglobin is binded to oxygen, is reached at 2 torr which is relatively low compared to 26 torr for hemoglobin. (wikibooks.org)
  • Lorilee S. L. Arakaki, Martin J. Kushmerick, and David H. Burns, "Myoglobin Oxygen Saturation Measured Independently of Hemoglobin in Scattering Media by Optical Reflectance Spectroscopy," Appl. (osapublishing.org)
  • Partial least-squares (PLS) and second-derivative preprocessing were used to obtain estimates of myoglobin oxygen fractional saturation from diffuse reflectance spectra of solutions containing myoglobin, hemoglobin, and a scatterer. (osapublishing.org)
  • myoglobin fractional saturation varies between 0 and 1. (osapublishing.org)
  • Myoglobin is hyperbolic curve Total oxygen saturation doesn't change much between lungs and tissue. (coursehero.com)
  • Myoglobin is oxygen storage Hemoglobin is sigmodal curve Saturation of hemoglobin in tissues is different from the saturation levels in the lungs. (coursehero.com)
  • Molecular orbital description of Fe-O 2 interaction in myoglobin. (wikipedia.org)
  • This is the first time that a disease caused by a mutation in the myoglobin gene has been identified', says Montse Olivé, doctor at the Bellvitge University Hospital, responsible for the muscular disease area and researcher of the Human Molecular Genetics group of the Genes, Disease and Therapy at IDIBELL. (news-medical.net)
  • Myoglobin, molecular model. (sciencephoto.com)
  • Myoglobin heme free Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 11.67 kDa. (prospecbio.com)
  • Molecular weight of Myoglobin was determined by running SDS-PAGE. (ukessays.com)
  • Due to its low molecular weight, myoglobin is released more rapidly when muscle cells are damaged than other markers. (rapidtest.com)
  • The mutant L29F of myoglobin [1], in which a leucine residue is replaced by a phenylalanin, proved to be an interesting test case because substantial protein conformational changes take place during the first few hundred picoseconds after laser photolysis. (esrf.eu)
  • To facilitate interpretation of functional data, structures of several mutant myoglobins have been determined by X-ray crystallography. (rice.edu)
  • In contact with venous blood, oxygen combines more readily with myoglobin than it does with hemoglobin, favouring the transfer of oxygen from blood to muscle cells. (britannica.com)
  • The myoglobin blood test measures the level of the protein myoglobin in the blood. (medlineplus.gov)
  • Like haemoglobin which are the oxygen carrying pigments in red blood, myoglobin take up and subsequently store oxygen that it releases when muscle tissues need oxygen in order to sustain contraction. (answers.com)
  • A myoglobin blood test may be used detect muscle damage. (labcorp.com)
  • When heart or skeletal muscle is injured, myoglobin is released into the blood. (labcorp.com)
  • Myoglobin combines with oxygen released by red blood cells and transfers it to the mitochondria of muscle cells, where it is used to produce energy. (dictionary.com)
  • 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 - therefore giving us a possibility of staying underwater longer - a helpful remedy for one of the harry potter tasks in the 4th film/book! (thenakedscientists.com)
  • CTSO ), a critical care immunotherapy leader using its CytoSorb® blood purification technology to treat deadly inflammation in critically-ill and cardiac surgery patients around the world, announced that it has received European Union regulatory approval to expand the use of CytoSorb to reduce elevated bilirubin and myoglobin from blood. (prnewswire.com)
  • The system studied by this team, the oxygen storage protein myoglobin, is similar to hemoglobin but is found in muscle cells rather than blood cells. (esrf.eu)
  • 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)
  • This test measures the amount of a protein called myoglobin in your blood. (ahealthyme.com)
  • When you have a heart attack or severe muscle damage, myoglobin is released into your blood. (ahealthyme.com)
  • Myoglobin increases in your blood 2 to 3 hours after the first symptoms of muscle damage. (ahealthyme.com)
  • Myoglobin is a sensitive marker for muscle injury and can be used as a potential marker in the blood for detection of heart attacks. (leebio.com)
  • Myoglobin test is carried out with the help of a blood sample. (transparencymarketresearch.com)
  • In humans, myoglobin is only found in the bloodstream after muscle injury . (wikipedia.org)
  • When muscle is damaged, myoglobin in muscle cells is released into the bloodstream. (medlineplus.gov)
  • The only time myoglobin is found in the bloodstream is when it is released following muscle injury. (answers.com)
  • When myoglobin is found in the bloodstream, this is abnormal and can be diagnostically relevant 3 . (leebio.com)
  • The polypeptide chain is bound to a heme molecule which represents the prosthetic group of myoglobin. (doccheck.com)
  • Now, using an X-ray laser at the Department of Energy's SLAC National Accelerator Laboratory, researchers have for the first time directly seen myoglobin move within quadrillionths of a second after a bond breaks and the protein releases a gas molecule . (phys.org)
  • Other Cardiac Markers Rapid Tests such as Myoglobin Rapid Test, the CRP Serum Rapid Test are available, along with Cardiac Markers ELISA Tests. (rapidtest.com)