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.
Any normal or abnormal coloring matter in PLANTS; ANIMALS or micro-organisms.
The layer of pigment-containing epithelial cells in the RETINA; the CILIARY BODY; and the IRIS in the eye.
Photosensitive protein complexes of varied light absorption properties which are expressed in the PHOTORECEPTOR CELLS. They are OPSINS conjugated with VITAMIN A-based chromophores. Chromophores capture photons of light, leading to the activation of opsins and a biochemical cascade that ultimately excites the photoreceptor cells.
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.
Linear TETRAPYRROLES that give a characteristic color to BILE including: BILIRUBIN; BILIVERDIN; and bilicyanin.
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)
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Necrosis or disintegration of skeletal muscle often followed by myoglobinuria.
Chemical bond cleavage reactions resulting from absorption of radiant energy.
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
Coloration or discoloration of a part by a pigment.
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.
Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.
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.
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.
Chromatophores (large pigment cells of fish, amphibia, reptiles and many invertebrates) which contain melanin. Short term color changes are brought about by an active redistribution of the melanophores pigment containing organelles (MELANOSOMES). Mammals do not have melanophores; however they have retained smaller pigment cells known as MELANOCYTES.
The large pigment cells of fish, amphibia, reptiles and many invertebrates which actively disperse and aggregate their pigment granules. These cells include MELANOPHORES, erythrophores, xanthophores, leucophores and iridiophores. (In algae, chromatophores refer to CHLOROPLASTS. In phototrophic bacteria chromatophores refer to membranous organelles (BACTERIAL CHROMATOPHORES).)
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 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).
Large mammals in the family Elephantidae, with columnar limbs, bulky bodies, and elongated snouts. They are the only surviving members of the PROBOSCIDEA MAMMALS.
Photosensitive proteins expressed in the ROD PHOTORECEPTOR CELLS. They are the protein components of rod photoreceptor pigments such as RHODOPSIN.
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.
An essential amino acid that is required for the production of HISTAMINE.
Insoluble polymers of TYROSINE derivatives found in and causing darkness in skin (SKIN PIGMENTATION), hair, and feathers providing protection against SUNBURN induced by SUNLIGHT. CAROTENES contribute yellow and red coloration.
A potent liver poison. In rats, bromotrichloromethane produces about three times the degree of liver microsomal lipid peroxidation as does carbon tetrachloride.
A naturally occurring lipid pigment with histochemical characteristics similar to ceroid. It accumulates in various normal tissues and apparently increases in quantity with age.
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 rate dynamics in chemical or physical systems.
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
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)
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
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).
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 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.
Inorganic salts of iodic acid (HIO3).
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)
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.
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.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A carotenoid constituent of visual pigments. It is the oxidized form of retinol which functions as the active component of the visual cycle. It is bound to the protein opsin forming the complex rhodopsin. When stimulated by visible light, the retinal component of the rhodopsin complex undergoes isomerization at the 11-position of the double bond to the cis-form; this is reversed in "dark" reactions to return to the native trans-configuration.
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.
Specialized cells that detect and transduce light. They are classified into two types based on their light reception structure, the ciliary photoreceptors and the rhabdomeric photoreceptors with MICROVILLI. Ciliary photoreceptor cells use OPSINS that activate a PHOSPHODIESTERASE phosphodiesterase cascade. Rhabdomeric photoreceptor cells use opsins that activate a PHOSPHOLIPASE C cascade.
A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.
Oxygenated forms of carotenoids. They are usually derived from alpha and beta carotene.
An oval area in the retina, 3 to 5 mm in diameter, usually located temporal to the posterior pole of the eye and slightly below the level of the optic disk. It is characterized by the presence of a yellow pigment diffusely permeating the inner layers, contains the fovea centralis in its center, and provides the best phototropic visual acuity. It is devoid of retinal blood vessels, except in its periphery, and receives nourishment from the choriocapillaris of the choroid. (From Cline et al., Dictionary of Visual Science, 4th ed)
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The thin, highly vascular membrane covering most of the posterior of the eye between the RETINA and SCLERA.
The general name for a group of fat-soluble pigments found in green, yellow, and leafy vegetables, and yellow fruits. They are aliphatic hydrocarbons consisting of a polyisoprene backbone.
Photosensitive afferent neurons located primarily within the FOVEA CENTRALIS of the MACULA LUTEA. There are three major types of cone cells (red, blue, and green) whose photopigments have different spectral sensitivity curves. Retinal cone cells operate in daylight vision (at photopic intensities) providing color recognition and central visual acuity.
The muscle pigment, myoglobin, provides an effective bond. This additional oxygen storage is vital for deep diving, since ...
It is a deeply colored pigment that is not soluble in basic water. The free porphyrin is encountered in nature in the form of ... These heme-containing proteins include hemoglobin, myoglobin, and cytochrome c. Complexes can also be formed with other metal ... A. R. Battersby; C. J. R. Fookes; G. W. J. Matcham; E. McDonald (1980). "Biosynthesis of the pigments of life: formation of the ...
The water-soluble proteins are sarcoplasmic proteins such as myoglobin and other pigments; salt-soluble proteins are ...
The carbon monoxide combines with myoglobin to form carboxymyoglobin, a bright-cherry-red pigment. Carboxymyoglobin is more ... stable than the oxygenated form of myoglobin, oxymyoglobin, which can become oxidized to the brown pigment metmyoglobin. This ... Carbon monoxide also binds to other molecules such as myoglobin and mitochondrial cytochrome oxidase. Exposures to carbon ...
Vermilion pigment, made from cinnabar. This was the pigment used in the murals of Pompeii and to color Chinese lacquerware ... Red meat gets its color from the iron found in the myoglobin and hemoglobin in the muscles and residual blood. Plants like ... pigments et teintures dans les mains des peuples. Seuil. ISBN 978-2-02-084697-4. Davies, Kevin M. (2004). Plant pigments and ... Red pigment made from ochre was one of the first colors used in prehistoric art. The Ancient Egyptians and Mayans colored their ...
He determined the properties and dissociation curve of myoglobin which explain the physiological function of the pigment. He ... He painted watercolours using pigments he himself extracted. In the 1920s, he developed a fish-eye camera and used it to take ...
Atlantic horseshoe crab blood Keyhole limpet hemocyanin Hemoglobin Myoglobin Respiratory pigment Coates CJ, Nairn J (July 2014 ...
The pigment commonly used for this was called light cinabrese; it was a mixture of the red earth pigment called sinopia, or ... Pork contains less myoglobin than beef and therefore is less red; when heated, it changes from pinkish-red to less pink to tan ... Pigments - Pinke[edit]. Main article: Pinke (color). In the 17th century, the word pink or pinke was also used to describe a ... And this pigment does you great credit if you use it for painting faces, hands and nudes on walls..."[12] ...
Pigments include those produced endogenously, such as hemoglobin in hemolytic anemia, myoglobin in rhabdomyolysis, and ... Drug pigments, such as phenazopyridine, may also cause cast discoloration. Though crystallized urinary solutes, such as ... Formed by the adhesion of metabolic breakdown products or drug pigments, these casts are so named due to their discoloration. ...
... pigments and less myoglobin than unprocessed dark meats. Meat slurry is more malleable than dark meats and eases the process of ... are caused by myoglobin, a pigmented chemical compound found in muscle tissue that undergoes frequent use. Because domestic ... The mixture is then used in a centrifuge or with an emulsifier to separate the fats and myoglobin from the muscle. The product ... Dark meat which is high in myoglobin is less useful in industry, especially fast food, because it is difficult to mold into ...
As the muscle pigment myoglobin denatures, its iron oxidates, which may cause a brown discoloration near the surface of the ... When myoglobin is exposed to oxygen, reddish oxymyoglobin develops, making myoglobin-rich meat appear red. The redness of meat ... Meat can be broadly classified as "red" or "white" depending on the concentration of myoglobin in muscle fibre. ...
... as the lower temperature of the middle of the steak was not sufficient to cause the myoglobin to lose its pigment. When smoking ... The pinkish color in meat is typically due to the presence of a compound called myoglobin. Myoglobin typically darkens and ... The NO combined with the myoglobin form a stable pink molecule that does not denature in the heat. The depth of the smoke ring ... allows smoke to penetrate the meat and react with the myoglobin before the temperature causes a reaction with it causing it to ...
Myoglobin was demonstrated in the urine of victims by spectroscopy, and it was noted that the kidneys of victims resembled ... If kidney damage has occurred, microscopy of the urine also reveals urinary casts that appear pigmented and granular. ... The urine may be dark, often described as "tea-colored", due to the presence of myoglobin. Damage to the kidneys may give rise ... Some of the muscle breakdown products, such as the protein myoglobin, are harmful to the kidneys and may lead to kidney failure ...
"Meat Pigment Chemistry", taken from IFT Mini-Experiments in Food Science Series" (PDF). Sindelar, Jeffrey; Milkowski, Andrew ( ... Nitrite reacts with the meat myoglobin to cause color changes, first converting to nitrosomyoglobin (bright red), then, on ... Bailey, M. E.; Frame, R. W.; Naumann, H. D. (January 1964). "Cured Meat Pigments, Studies of the Photooxidation of ... which has the ability to transfer nitric oxide that subsequently reacts with myoglobin to produce the cured meat color. The ...
Such rosy pigmentation is produced by a direct chemical reaction of nitric oxide with myoglobin to form nitrosomyoglobin, ... followed by concentration of the pigments due to drying. Bacteria convert the added nitrite or nitrate to nitric oxide. Sliced ...
3/3 Phytoglobins (myoglobin-like family) Phytogb0: the basal type, found in algae, bryophytes and gymnosperms. Phytogb1, 2: ... discovered in 1939 by Kubo after spectroscopic and chemical analysis of the red pigment of soybean root nodules. A few decades ... The first and third intron of the phytogb genes are localized in the same position as that of the myoglobin genes, which ... by Vainshtein and collaborator revealed that the tertiary structure of this protein and that of the sperm whale myoglobin was ...
... s are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of ... other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric ... Battersby, Alan R. (2000). "Tetrapyrroles: The pigments of life". Natural Product Reports. 17 (6): 507-526. doi:10.1039/ ...
This is necessary because the dark meat requires a higher temperature to denature all of the myoglobin pigment than the white ... meat (which is very low in myoglobin), so that fully cooking the dark meat tends to dry out the breast. Brining makes it ...
... and myoglobin, the red pigment that stores oxygen until needed for muscular activity. There are three types of myofilaments: ... Type I fibers appear red due to the high levels of myoglobin. Red muscle fibers tend to have more mitochondria and greater ... Well exercised muscles can not only add more size but can also develop more mitochondria, myoglobin, glycogen and a higher ... They contain high mitochondrial volumes, and the high levels of myoglobin that give them a red pigmentation. They have been ...
Acute tubular necrosis occurs when PTECs are directly damaged by toxins such as antibiotics (e.g., gentamicin), pigments (e.g ... myoglobin) and sepsis (e.g., mediated by lipopolysaccharide from gram-negative bacteria). Renal tubular acidosis (proximal type ...
... a red pigment when included inside myoglobin, and a pink pigment when it has been released by cooking. It participates to the " ...
... myoglobin -- absorption spectrum -- action spectrum -- fluorescence Photosynthesis : light reaction -- dark reaction ... pigments : chlorophyll -- carotenoids -- xanthophyll -- cytochrome -- phycobilin -- bacteriorhodopsin -- hemoglobin -- ...
The next step is the reduction of biliverdin to a yellow color tetrapyrol pigment called bilirubin by cytosolic enzyme ... such as muscle myoglobin and cytochromes. The unconjugated bilirubin then travels to the liver through the bloodstream. Because ... However, the sclera themselves are not "icteric" (stained with bile pigment) but rather the conjunctival membranes that overlie ... Unconjugated bilirubin comes from the breakdown of the heme pigment found in red blood cells' hemoglobin. The increased ...
Sidell, B. D. & Kristin M. O'Brien (2006). "When bad things happen to good fish: The loss of hemoglobin and myoglobin ... Ruud, Johan T. (1954). "Vertebrates without erythrocytes and blood pigment". Nature. 173 (4410): 848-50. Bibcode:1954Natur.173 ...
... contains hemes, pigments responsible for the colour of red meat. The colour that meat takes is partly determined by ... 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 ... All known vertebrate myoglobins and β-hemoglobin subunits are similar in structure, but myoglobin binds O2 more avidly at low ... Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not ...
Thus, in properly bled muscle tissue myoglobin is responsible for 90% or more of the pigmentation. The myoglobin quantity ... Biological pigments include plant pigments and flower pigments. Many biological structures, such as skin, eyes, feathers, fur ... which uses the green pigment chlorophyll and several colorful pigments that absorb as much light energy as possible. Pigments ... The principal pigments responsible are: Chlorophyll is the primary pigment in plants; it is a chlorin that absorbs blue and red ...
Leghemoglobin is a molecule similar in structure to myoglobin that is currently being used in artificial meat products, such as ... A respiratory pigment is a metalloprotein that serves a variety of important functions, its main being O2 transport. Other ... 1985). Respiratory pigments in animals: relation, structure-function. Berlin; New York: Springer-Verlag. ISBN 978-0-387-15629-3 ... Hemocyanin is a respiratory pigment that uses copper as its oxygen-binding molecule, as opposed to iron with hemoglobin. ...
The method does not involve the application of a dye, but rather causes the pigment Prussian blue to form directly within the ... the procedure does not stain iron that is bound to porphyrin forming heme such as hemoglobin and myoglobin. The stain is an ... Potassium ferrocyanide in the staining solution combines with the ferric iron forming the Prussian blue pigment. The addition ... then react with the soluble ferrocyanide in the stain to form the insoluble Prussian blue pigment (a complex hydrated ferric ...
... haemoglobin and myoglobin store oxygen in body tissue; and they have twice the concentration of myoglobin than haemoglobin. ... Whales do, however, lack short wavelength sensitive visual pigments in their cone cells indicating a more limited capacity for ... Norena, S. R.; Williams, T. M. (2000). "Body size and skeletal muscle myoglobin of cetaceans: adaptations for maximizing dive ...
Lecture - 12 Myoglobin and Hemoglobin on YouTube *^ Biochemistry (Eighth ed.). New York: W. H. Freeman. 2015-04-08. ISBN ... When the porphyrin ring is broken up, the fragments are normally secreted as a yellow pigment called bilirubin, which is ... 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 ...
Myoglobin, a compound related to hemoglobin, acts to store oxygen in muscle cells.[10] ... Ruud JT (May 1954). "Vertebrates without erythrocytes and blood pigment". Nature. 173 (4410): 848-50. Bibcode:1954Natur.173.. ...
... is the primary oxygen-carrying pigment of muscle tissues.[7] High concentrations of myoglobin in muscle cells allow ... Myoglobin contains hemes, pigments responsible for the colour of red meat. The colour that meat takes is partly determined by ... 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), ...
The body of an adult human contains about 4 grams (0.005% body weight) of iron, mostly in hemoglobin and myoglobin. These two ... Iron(III) oxide and oxyhidroxide are used as reddish and ocher pigments. ... Thus, when deoxyhemoglobin takes up oxygen, its affinity for more oxygen increases, and vice versa.[136] Myoglobin, on the ... and pigments. The best known sulfide is iron pyrite (FeS2), also known as fool's gold owing to its golden luster.[50] It is not ...
These molecules are an important component of the hemoproteins, such as hemoglobin, myoglobin and various cytochromes.[37] ... pigments Hemes Cobalamins (vitamin B12) Various. vitamin Bs Calciferols. (vitamin D) ...
Haem is synthesised in every energy-producing cell in the body and is a key structural component of haemoglobin, myoglobin and ... This absorption in the near infrared region makes NCs candidates for highly pigmented tumours, including melanomas, which ...
... and myoglobin, the red pigment that stores oxygen until needed for muscular activity.[7] ... 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 ...
The muscle pigment, myoglobin, provides an effective bond. This additional oxygen storage is vital for deep diving, since ...
... s are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of ... other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric ...
"In recognition of his distinguished work on the visual pigments in the living eye and on chemical and nervous adaptation in the ... "In recognition of his distinguished contributions to the complete structural analysis of a protein molecule (myoglobin), ...
Their hemoglobin and myoglobin store oxygen in body tissues and they have twice the concentration of myoglobin than hemoglobin. ... Dolphins do, however, lack short wavelength sensitive visual pigments in their cone cells indicating a more limited capacity ... Norena, S. R.; Williams, T. M. (2000). "Body size and skeletal muscle myoglobin of cetaceans: adaptations for maximizing dive ...
Myoglobin, which is similar to haemoglobin, is the main oxygen-carrying pigment of muscle tissues.[1] Like haemoglobin, it has ... 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 ... Myoglobin is a protein that is able to bind oxygen. ... Myoglobin. From Simple English Wikipedia, the free encyclopedia ...
Hemoglobin and myoglobin are two O2-binding proteins that contain iron porphyrins. Various cytochromes are also hemoproteins. A ... One of the best-known families of porphyrin complexes is heme, the pigment in red blood cells, a cofactor of the protein ... Bile pigments are the breakdown products of heme. The following scheme summarizes the biosynthesis of porphyrins, with ...
... while Max Perutz and John Kendrew analysed the 3D structure of myoglobin and later haemoglobin. These breakthroughs in protein ... P-granules Starch granules Glycogen granules Corneal lens formation and cataracts Other cytoplasmic inclusions such as pigment ...
Sidell, B and O'Brien, KM (2006). "When bad things happen to good fish: the loss of hemoglobin and myoglobin expression in ... While the majority of animal species have up to 45% of hemoglobin (or other oxygen-binding and oxygen-transporting pigments) in ...
1735 Swedish chemist Georg Brandt analyzes a dark blue pigment found in copper ore. Brandt demonstrated that the pigment ... specifically sperm whale myoglobin. 1962 Neil Bartlett synthesizes xenon hexafluoroplatinate, showing for the first time that ... Observations and remarks concerning an extraordinary pigment - cobalt), Kongliga Svenska vetenskapsakademiens handlingar ( ...
Myoglobin, on the other hand, contains only one heme group and hence this cooperative effect cannot occur. Thus, while ... Iron(III) oxide and oxyhidroxide are used as reddish and ocher pigments. Iron(III) chloride finds use in water purification and ... The body of an adult human contains about 4 grams (0.005% body weight) of iron, mostly in hemoglobin and myoglobin. These two ... and pigments. The best known sulfide is iron pyrite (FeS2), also known as fool's gold owing to its golden luster. It is not an ...
... other globins with a hem group such as myoglobin can also catalyse the same reaction. The presence of myoglobin in urine gives ... Highly pigmented urine and contamination of the container with quaternary ammonium compounds, detergents and antiseptics also ... The presence of myoglobin in place of hemoglobin can be caused by pathologies associated with muscular damage (rhabdomyolysis ... Analysis of the supernatant for blood with a test strip will give a positive if myoglobin is present and a negative if ...
1954). Vertebrates without erythrocytes and blood pigment. Nature 173, 848-.. OpenUrlCrossRefPubMed ... 1986). Myoglobin expression: early induction and subsequent modulation of myoglobin and myoglobin mRNA during myogenesis. Mol. ... Concentrations of myoglobin and myoglobin mRNA in heart ventricles from Antarctic fishes ... Concentrations of myoglobin and myoglobin mRNA in heart ventricles from Antarctic fishes ...
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 ... Like haemoglobin which are the oxygen carrying pigments in red blood, myoglobin take up and subsequently store oxygen that it ... What is the role of the Myoglobin? Myoglobin is a monomeric heme protein found mainly in muscle tissue where it serves as an ...
Examples: chlorophyll; canthaxanthin; anthocyanin; rhodopsin; myoglobin. Organic pigments - Pigment Red 170; Indian Yellow; ... The appearance of pigments is intimately connected to the color of the source light. Pigments are water-and oil-insoluble ... Classification of Pigments. Biological pigments - used in biological process like Camouflage, Mimicry, Aposematism and Sexual ... Both dyes and pigments appear to be colored as a result of absorption of some wavelengths of light more than others. ...
Myoglobin is a richly pigmented protein. The more myoglobin there is in the cells, the redder, or darker, the meat. ... Rare beef is cooked to 140° F, and myoglobins red color remains unchanged. Above 140° F, myoglobin loses its ability to bind ... The protein myoglobin stores oxygen in muscle cells, which use oxygen to extract the energy needed for constant activity. ... When the interior of the meat reaches 170° F, hemichrome levels rise, and the myoglobin becomes metmyoglobin, which gives well- ...
... as well as the pigment that makes the blood appear red. The destruction of blood cells within the blood vessels frees ... Bilirubin is a red-yellow bile pigment that comes from the degradation of the red pigment (heme) in hemoglobin; too much ... Myoglobin serves the same purpose as hemoglobin but is particular to the muscles, and is differentiated by the amount of oxygen ... If there is too much hemoglobin and myoglobin in the blood plasma, these proteins will no longer be reabsorbed in the kidneys, ...
The muscle pigment, myoglobin, provides an effective bond. This additional oxygen storage is vital for deep diving, since ...
Pigment or uric acid exposure can be treated with alkaline diuresis. Ethylene glycol or methanol poisoning should be treated ... Elevated creatine kinase level, elevated myoglobin level. Rhabdomyolysis. Elevated uric acid level ...
Pigmented areas are assymetric, irregular boarders, vary in color, diameter greater than 6mm than its cancerous ... Whats the advantage of having both hemoglobin and myoglobin in muscles Reduces the needs of muscles to have continuous blood ...
Provides pigment for skeletal muscle. Myoglobin. ___ is recording of the contractions of muscle. Myogram. ...
An iron-containing red pigment found in muscle fibers. Myoglobin. What is made up of spindle-shaped cells with a single nucleus ... An iron-containing pigment found in red blood cellsCarries about 97% of the oxygen in the body. Hemoglobin. ...
Avian striated muscles contain a respiratory pigment, myoglobin. There are relatively few myoglobin-containing cells in "white ...
It is a deeply colored pigment that is not soluble in basic water. The free porphyrin is encountered in nature in the form of ... These heme-containing proteins include hemoglobin, myoglobin, and cytochrome c. Complexes can also be formed with other metal ... A. R. Battersby; C. J. R. Fookes; G. W. J. Matcham; E. McDonald (1980). "Biosynthesis of the pigments of life: formation of the ...
myoglobin. Definition. red pigment in slow fibers; related to hemoglobin; binds oxygen molecules. ...
Myoglobin. Definition. red pigment that stores oxygen. Term. Myofibrils. Definition. long strands of protein. ...
Study Cell Injury: Necrosis and Apoptosis flashcards from Madeline Libin
Iron is an essential component of the respiratory pigments haemoglobin and myoglobin. ... Copper is also believed to be necessary for the formation of the pigment melanin and consequently skin pigmentation, for the ... As a component of the respiratory pigments and enzymes concerned in tissue oxidation, iron is essential for oxygen and electron ... Minerals serve as essential components of many enzymes, vitamins, hormones, and respiratory pigments, or as cofactors in ...
... urine myoglobin explanation free. What is urine myoglobin? Meaning of urine myoglobin medical term. What does urine myoglobin ... Looking for online definition of urine myoglobin in the Medical Dictionary? ... The color of urine is due to the presence of the yellow pigment urochrome. Individual ingredients of urine are not usually ... redirected from urine myoglobin). Also found in: Dictionary, Thesaurus, Encyclopedia.. Related to urine myoglobin: ...
Myoglobin contains hemes, pigments responsible for the colour of red meat. The colour that meat takes is partly determined by ... 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 ... All known vertebrate myoglobins and β-hemoglobin subunits are similar in structure, but myoglobin binds O2 more avidly at low ... Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not ...
MYOGLOBINMyoglobin is a haemoglobin-like, iron-containing pigment found in muscle fibres. • It consists of a single alpha ... Myoglobin takes up oxygen from the haemoglobin in the blood and stores oxygen within the muscle itself. ... The oxygen dissociation curve for myoglobin is hyperbolic (as opposed to the sigmoidal curve for haemoglobin) and is to the ...
Myoglobin was discovered spectroscopically by Mörner in 1897 (Mörner, 1897). In order to distinguish this muscle pigment - ... 1970). Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. Physiol. Rev. 50, 559-636. ... The role of myoglobin during parasite infection under normoxic conditions. Beyond the initial finding of the role of myoglobin ... The role of myoglobin in renal failure and myocardial ischemia/reperfusion injury. It has been suggested that myoglobin might ...
This colour is due to the pigment myoglobin loosely binding oxygen to form oxymyoglobin. For this colour to develop and be ... After a time the cut surface becomes more brown as a result of myoglobin binding the oxygen more tightly to form metmyoglobin. ...
The Myoglobin heme free contains N-terminal T7 tag and purified by proprietary chromatographic techniques. ... Recombinant Human Myoglobin heme free produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of ... Myoglobin is responsible for the pigments that make meat red. The color of the meat is partly determined by the charge of the ... Myoglobins molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of ...
... is what gives meat its red pigment. What is less well-known is that in 1957, it became the first protein molecule whose ... Myoglobin, a protein in muscle tissue that stores oxygen, ... Myoglobin, a protein in muscle tissue that stores oxygen, is ... SLACs X-ray laser enables direct images of ultrafast structural changes in myoglobin. by SLAC National Accelerator Laboratory ... Years of improvements and development of liquid jets that delivered the tiny crystals of myoglobin to the X-rays, and ...
This muscle contains myoglobin, an oxygen-carrying pigment. Red muscle functions for cruising. ...
Iron is also needed for myoglobin to form. Myoglobin is found in muscle tissue. It supplies oxygen to working muscle cells. It ... This is the red pigment inside red blood cells that gives blood its color. Iron is stored by the body in the liver, spleen, and ...
Pigments: hemoglobin, myoglobin. *Tumor Lysis Syndrome. *Crystals-oxalate or uric acid. Intrinsic Renal Etiologies*Acute ...
Orange-red pigmented casts in renal tubular lumens were strongly immunolabeled for myoglobin. To our knowledge, this is the ... Using immunohistochemistry, degenerate myofibers with depletion of myoglobin, and an intracytoplasmatic immunoreaction for ... KEYWORDS: Capture myopathy, cetaceans, Dolphin, fibrinogen, myoglobin, myoglobinuric nephrosis, rhabdomyolysis, Stenella ...
Obtain confirmation in the laboratory that the pigment is hemoglobin and not myoglobin. This can be accomplished easily because ... but two thirds of body iron is derived from dietary myoglobin and hemoglobin. Heme iron is not chelated and precipitated by ...
PHOTO : Figure 1 Formation of cooked cured-meat pigment (CCMP) from myoglobin and nitrite. Symbol P denotes protein. Hemoglobin ... The colour of raw meat comes from its hemoproteins, principally myoglobin. Myoglobin is composed of a protein, globin, and an ... The preformed cooked cured-meat pigment, similar to the pigment present in nitrite-cured meats, undergoes decomposition. Its ... This pigment may also be produced from hemoglobin prepared from bovine or porcine blood, after plasma separation and as ...
  • In fact, gradations of redness in meat are directly related to the concentration of myoglobin in the muscle fibers. (pressherald.com)
  • Under physiologic circumstances, the plasma concentration of myoglobin is very low (0 to 0.003 mg per dL). (aafp.org)
  • Collaborating with the University of Manitoba and University of Alaska, the researchers found a high concentration of myoglobin, the substance that makes meat look red, in the muscles of the mammalian divers. (digitaljournal.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)
  • High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. (wikipedia.org)
  • Myoglobin is released from damaged muscle tissue (rhabdomyolysis), which has very high concentrations of myoglobin. (wikipedia.org)
  • Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. (prospecbio.com)
  • Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. (prospecbio.com)
  • 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)
  • It was shown in Chapter IV that severely wounded men commonly excrete heme-containing pigments, either hemoglobin or myoglobin, in the urine and that such excretion was constantly observed in patients destined to develop the syndrome of posttraumatic renal insufficiency. (army.mil)
  • A red or red-brown (abnormal) color could be from a food dye, eating fresh beets, a drug, or the presence of either hemoglobin or myoglobin. (naturalhealthtechniques.com)
  • The more myoglobin there is in the cells, the redder, or darker, the meat. (exploratorium.edu)
  • When the interior of the meat reaches 170° F, hemichrome levels rise, and the myoglobin becomes metmyoglobin, which gives well-done meat its brown-gray shade. (exploratorium.edu)
  • There are relatively few myoglobin-containing cells in "white meat ," whereas "dark meat" derives its characteristic colour from their presence. (britannica.com)
  • Myoglobin contains hemes, pigments responsible for the colour of red meat. (wikipedia.org)
  • The colour that meat takes is partly determined by the degree of oxidation of the myoglobin. (wikipedia.org)
  • Furthermore, if you've ever wondered why a veal chop is lighter in color than a steak, this is because as an animal's age increases, its myoglobin content goes up, leading to darker-colored, or redder, meat. (pressherald.com)
  • Pigs' muscles do contain myoglobin, although not nearly as much as cattle, so pork "" despite being called "the other white meat" "" falls somewhere in the middle of the spectrum. (pressherald.com)
  • Lastly, if you're wondering why heat changes the color of meat, to put things simply, when red meat is cooked, the structure of its myoglobin is altered, leading to a color change "" from red to brown. (pressherald.com)
  • The protein myoglobin is the major pigment found in all vertebrates and can exist in various forms which determine the resulting meat color. (usda.gov)
  • The major reason that poultry meat is much lighter in color than beef is that it is dramatically lower in myoglobin. (usda.gov)
  • The pink, red or white coloration of meat is due primarily to oxygen-storing myoglobin which is located in the muscle cells and retains the oxygen brought by the blood until the cells need it. (usda.gov)
  • Myoglobin is responsible for the pigments that make meat red. (prospecbio.com)
  • The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. (prospecbio.com)
  • Myoglobin, a protein in muscle tissue that stores oxygen, is what gives meat its red pigment. (phys.org)
  • The present inventors found that a natural red pigment can be obtained from hemoglobin and myoglobin whose metalloporphyrin moiety is zinc protoporphyrin, and made meat products, whale meat products, fish meat products and fish paste products that were colored with the natural red pigment. (google.com)
  • myoglobin (oxygen-carrying molecules in muscle) and makes up around half the iron found in red meat, poultry and fish. (scribd.com)
  • Discolouration caused by oxidation of the red pigment in meat is a particular challenge. (linde-gas.com)
  • They all start with a meat protein called myoglobin. (nytimes.com)
  • Myoglobin stays unchanged and red as the meat juices flow, then turns from red to gray-brown as the release of moisture ends and the meat becomes dry. (nytimes.com)
  • Because myoglobin exposed to air eventually turns brown, red surfaces on raw meat also signify freshness. (nytimes.com)
  • A study published last September in the Journal of Agricultural and Food Chemistry showed that added lactate revives an enzyme system in the meat itself that constantly regenerates the normal myoglobin pigment and keeps it red. (nytimes.com)
  • Nitrite reacts in the meat tissue to form nitric oxide, which binds tightly to the iron in myoglobin and turns it a stable red. (nytimes.com)
  • This is because the colour of meat depends mainly on the pigment myoglobin. (ampc.com.au)
  • Blooming is the oxygenation of the myoglobin at the meat surface and is represented by the colour changing to red. (ampc.com.au)
  • Myoglobin, the respiratory pigment in muscle, gives a freshly cut piece of meat its dark red color. (thefreedictionary.com)
  • Fresh meat appears red because of the way its natural pigments (myoglobin) interact with oxygen. (mpi.govt.nz)
  • Fourth, the ribs develop a "smoke ring," a ring of pink just below the surface of the meat, caused by the interaction of its red pigment with nitric oxide or carbon monoxide from the grill. (seriouseats.com)
  • Sodium or potassium nitrite reduces to nitric oxide (a gas) and binds to myoglobin, the color pigment in meat. (theingredientstore.com)
  • Such pigments include myoglobin, released from skeletal muscle in rhabdomyolysis, and hemoglobin, released during intravascular hemolysis. (neurologyadvisor.com)
  • The aim of this study was to evaluate the role of urinary dipstick test in the detection of haeme pigment in patients who were at risk of acute renal failure (ARF) due to rhabdomyolysis after suffering injury in the Bam earthquake. (who.int)
  • Furthermore, the impact of myoglobin on parasite infection, rhabdomyolysis, hindlimb and liver ischemia, angiogenesis and tumor growth are considered. (biologists.org)
  • Rhabdomyolysis occurs when skeletal muscles are damaged and release myoglobin into the bloodstream. (winchesterhospital.org)
  • Ultimately, URMC physicians diagnosed him with rhabdomyolysis , the breakdown of muscle fibers that results in the release of a potentially harmful protein pigment called myoglobin into the bloodstream. (healthcanal.com)
  • 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. (biologists.org)
  • Highly pigmented meats, such as beef, require higher oxygen concentrations than meats with low pigmentation levels such as pork. (linde-gas.com)
  • Moreover, lutein and zeaxanthin are antioxidants, which help protect the macula from oxidative stress, and larger plasma concentrations of these pigments may lower the risk of age-related macular degeneration. (thefreedictionary.com)
  • or concentrations of raw patty heme and nonhemeiron, myoglobin, and total pigment. (k-state.edu)
  • Published in Science Magazine , the scientists say high muscle myoglobin concentrations in particular are mechanistically linked with an extended dive capacity phenotype, yet little is known regarding the molecular and biochemical underpinnings of this key specialization. (digitaljournal.com)
  • But sometimes muscle destruction doesn't make itself known until enough damaged muscle fibers have released a pigmented protein called myoglobin into the blood and eventually into the kidneys and urine. (mda.org)
  • The protein myoglobin stores oxygen in muscle cells, which use oxygen to extract the energy needed for constant activity. (exploratorium.edu)
  • important for making hemoglobin, the oxygen-carrying red pigment in blood, and myoglobin, a pigment that stores oxygen in muscles. (babycenter.com)
  • Like the hemoglobin in blood, myoglobin is a molecule that stores oxygen, and it has an iron atom at its center to which the oxygen can bind. (nytimes.com)
  • Just like how we humans have hemoglobin, the whales have a pigment called myoglobin which stores oxygen in the muscles during times of deep dives. (sooperarticles.com)
  • Consequently, plasma color does not change, and the myoglobin is quickly cleared from the blood by the liver and kidneys. (petmd.com)
  • 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)
  • 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)
  • 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)
  • The importance of pigment mobilization, its transport via the plasma to the kidneys, and its excretion in the urine was therefore obvious early in our investigations, and the present chapter will be devoted to presentation of the available data and discussion of their significance. (army.mil)
  • Myoglobin is an iron-containing pigment that can cause severe damage to the kidneys. (winchesterhospital.org)
  • Hydration helps to quickly flush myoglobin out of the kidneys to restore their function. (winchesterhospital.org)
  • 6 The circulating myoglobin becomes "free" and is filtered by the kidneys. (aafp.org)
  • The only time myoglobin is found in the bloodstream is when it is released following muscle injury. (answers.com)
  • It is a primary oxygen-carrying pigment of muscle tissues and is related to … hemoglobin, but only found in the bloodstream after a muscle injury. (answers.com)
  • In humans, myoglobin is only found in the bloodstream after muscle injury. (wikipedia.org)
  • In addition to transporting oxygen through the bloodstream, iron is also a component of myoglobin, a pigment which functions in the muscles in a similar fashion to haemoglobin in the blood, allowing muscle cells to retain oxygen. (advertiser.ie)
  • These heme-containing proteins include hemoglobin, myoglobin, and cytochrome c. (wikipedia.org)
  • Muscle damage releases myoglobin into the blood plasma, but it does not bind to serum proteins. (petmd.com)
  • 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)
  • For more than 100 years, myoglobin has been among the most extensively studied proteins. (biologists.org)
  • 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)
  • Myoglobin released from damaged or necrotic muscle → binds to plasma proteins → excreted in urine before reaching levels that would discolor plasma. (vetstream.com)
  • He studies the mechanism of activation of visual pigments, the mechanisms of function of the plant regulatory protein phytochrome and a variety of heme proteins, such as myoglobin, hemoglobin, and cytochrome c oxidase, as well as the early events in the folding of a variety of proteins and DNA. (lifeboat.com)
  • Detrimental and beneficial effects of the presence of myoglobin are discussed for various states of tissue oxygen tension within the heart and skeletal muscle. (biologists.org)
  • Presence of myoglobin (muscle pigment) in the urine. (vetstream.com)
  • dark urine that looks like cola (indicating the presence of myoglobin protein), hours after exercising (seek medical care immediately if this occurs). (mda.org)
  • With muscle injury, large quantities of potassium, phosphate, myoglobin, creatine kinase (CK) and urate leak into the circulation. (aafp.org)
  • A positive urine myoglobin test provides supportive evidence. (aafp.org)
  • Like hemoglobin, myoglobin is a cytoplasmic protein that binds oxygen on a heme group. (wikipedia.org)
  • Pigs' muscles do contain myoglobin, but the concentration is not as heavy as it is in beef. (exploratorium.edu)
  • Avian striated muscles contain a respiratory pigment, myoglobin . (britannica.com)
  • 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)
  • Hence diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. (answers.com)
  • Myoglobin serves the same purpose as hemoglobin but is particular to the muscles, and is differentiated by the amount of oxygen and carbon monoxide it delivers to the tissues (more, and less, respectively). (petmd.com)
  • Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. (prospecbio.com)
  • Tests with known mixtures of the two pigments showed that the separation was approximately 80-percent effective, and analyses of normal and decolorized muscles from patients who died of the crush syndrome provided further confirmation of the validity of the method. (army.mil)
  • Iron is also found in myoglobin, which supplies oxygen to muscles, and in compounds that keep the immune system strong. (earthturns.com)
  • Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. (answers.com)
  • Myoglobin is a protein found in muscle tissue of vertebrates that is iron- and oxygen-binding. (answers.com)
  • Myoglobin has 8 alpha helices and a hydrophobic core. (prospecbio.com)
  • Myoglobin also contains iron-rich red pigments called hemes, which give these fibers their deep-red color. (pressherald.com)
  • Pigment nephropathy is an abrupt decline in renal function as a consequence of the toxic action of endogenous hem-containing pigment on the kidney. (neurologyadvisor.com)
  • Myoglobin is extremely toxic to renal tubules, and myoglobinuria may result in acute renal failure Kidney: acute kidney injury (AKI) . (vetstream.com)
  • In Chapter IX the significance of pigment excretion will be further emphasized by demonstrating that pigment precipitation in the lower segments of the nephrons was a constant feature of the renal lesion observed in fatal cases. (army.mil)
  • Myoglobin in the renal glomerular filtrate can precipitate and cause renal tubular obstruction, leading to renal damage. (aafp.org)
  • macular pigment A yellow pigment, insensitive to light with a maximum absorption around 460 nm, and located in the inner layers of the macular area of the retina. (thefreedictionary.com)
  • retinal pigments , visual pigments the photopigments in retinal rods and cones that respond to certain colors of light and initiate the process of vision. (thefreedictionary.com)
  • Minerals serve as essential components of many enzymes, vitamins, hormones, and respiratory pigments, or as cofactors in metabolism, catalysts and enzyme activators. (fao.org)
  • bile pigment any of the coloring matters of the bile , derived from heme , including bilirubin , biliverdin , and several others. (thefreedictionary.com)
  • Fast-twitch fibers, on the other hand, are anaerobic, contain less myoglobin and are lighter in color. (pressherald.com)
  • Myoglobin does help to transport oxygen in oxidative muscle tissue, but does not directly play a role in contraction. (answers.com)
  • Myoglobin is a monomeric heme protein found mainly in muscle tissue where it serves as an intracellular storage site for oxygen. (answers.com)
  • Myoglobin is found in muscle tissue. (ahealthyme.com)
  • In this review, we examine the functions of myoglobin for a variety of diseases depending on the oxygen tension of the tissue with regard to its beneficial as well as potential deleterious effects. (biologists.org)
  • Instead, the binding of oxygen by myoglobin is uninfluenced by the oxygen pressure in the surrounding tissue. (prospecbio.com)
  • e) means for multiplying said rate of decay by a conversion factor, and means for determining said concentration of a tissue pigment with a known absorption spectrum. (google.ca)
  • 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)
  • Hemoglobin is an oxygen carrier in the red blood cells, which also serves to carry oxygen to the tissues, as well as the pigment that makes the blood appear red. (petmd.com)
  • This is the red pigment inside red blood cells that gives blood its color. (ahealthyme.com)
  • In order to distinguish this muscle pigment - noted as muscle hemoglobin - from blood hemoglobin, Mörner first suggested the name myochrome. (biologists.org)
  • Iron is an essential component of the pigment haemoglobin, found in red blood cells. (scribd.com)
  • Iron is the main component needed for the production of haemoglobin, the pigment within our red blood cells, where it is required for oxygen transportation from the lungs to the body's tissues, and the carbon dioxide transportation from the tissues to the lungs. (advertiser.ie)
  • Chlorophyll gives leaves their green color Space-filling model of the chlorophyll molecule Chlorophyll is a green pigment found in most plants, algae, and cyanobacteria. (statemaster.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)
  • Myoglobin can take the forms oxymyoglobin (MbO2), carboxymyoglobin (MbCO), and metmyoglobin (met-Mb), analogously to hemoglobin taking the forms oxyhemoglobin (HbO2), carboxyhemoglobin (HbCO), and methemoglobin (met-Hb). (wikipedia.org)
  • Myoglobin exists in 3 different chemical forms and colours, deoxymyoglobin (purple), oxymyoglobin (red) and metmyoglobin (brown). (ampc.com.au)
  • When the pigment is fully oxidized, it converts to metmyoglobin, which has the typical brown color that consumers often regard as old beef. (ift.org)
  • Myoglobin contains a porphyrin ring with an iron at its center. (wikipedia.org)
  • Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. (prospecbio.com)
  • The exact mechanism of myoglobin causing defective glomerular filtration is not known. (scirp.org)
  • EPG or IFE to distinguish haemoglobin from myoglobin. (edu.au)
  • We were severely handicapped by the lack of a spectroscope of sufficient sensitivity to distinguish between the closely similar spectrums of hemoglobin and myoglobin, and even if a suitable instrument had been available it is doubtful if it could have been utilized under field conditions. (army.mil)
  • In the urine it did prove possible to distinguish between the two pigments within certain limits by taking advantage of the greater stability of myoglobin in alkaline solutions. (army.mil)
  • The presence of high levels of myoglobin, or some of its redder forms due to incomplete denaturation during heat processing, can account for poultry having a pink to red color similar to that of an undercooked product. (usda.gov)
  • When exposed to O 2 in air, the purple muscle pigment myoglobin becomes loosely oxygenated and converts to oxymyoglobin, an unstable bright cherry-red pigment that seems to signal freshness to most consumers. (ift.org)
  • The technology most used to retain the desired oxymyoglobin color is elevated O 2 atmosphere in the package, in the 80% concentration range, which converts myoglobin into oxymyoglobin. (ift.org)
  • Myoglobin is a haemoglobin-like, iron-containing pigment found in muscle fibres. (slideserve.com)
  • The oxygen dissociation curve for myoglobin is hyperbolic (as opposed to the sigmoidal curve for haemoglobin) and is to the left of that for haemoglobin. (slideserve.com)
  • Myoglobin's molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. (prospecbio.com)
  • Above 140° F, myoglobin loses its ability to bind oxygen, and the iron atom at the center of its molecular structure loses an electron. (exploratorium.edu)
  • 1987 ). Does myoglobin contribute significantly to diffusion of oxygen in red skeletal muscle? (biologists.org)
  • In vitro studies are concerned with the structural and genomic organization of myoglobin, its kinetic and dynamic behavior, and its binding, electrocatalytic and reduction properties. (biologists.org)
  • bioavailability via scavenging or formation, myoglobin serves as part of a sensitive dioxygen sensory system. (biologists.org)
  • Both dyes and pigments appear to be colored as a result of absorption of some wavelengths of light more than others. (medium.com)
  • Ink may be a liquid or paste form contains pigments or dyes. (medium.com)