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Topic: Myoglobin

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	MedlinePlus Medical Encyclopedia: Myoglobin - urine
		Urine myoglobin is a test to detect the presence of myoglobin in urine.
		Myoglobin is a protein in heart and skeletal muscles.
		Myoglobin has oxygen bound to it, thus providing an extra reserve of oxygen so that the muscle can maintain a high level of activity for a longer period of time.
	www.nlm.nih.gov /medlineplus/ency/article/003664.htm (571 words)

	Myoglobin Test: Encyclopedia of Medicine
		Myoglobin tests are done to evaluate a person who has symptoms of a heart attack (myocardial infarction) or other muscle damage.
		Myoglobin is one of the first tests done to determine if a person with chest pain is having a heart attack, as it may be one of the first blood tests to become abnormal.
		Myoglobin levels and levels of other cardiac markers are usually considered before finally confirming a diagnosis of heart attack.
	health.enotes.com /medicine-encyclopedia/myoglobin-test (659 words)

	Myoglobin - Wikipedia, the free encyclopedia
		Myoglobin is a single-chain globular protein of 153 amino acids, containing a heme (iron-containing porphyrin) prosthetic group in the center around which the remaining apoprotein folds.
		Myoglobin is often cited as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve.
		The released myoglobin is filtered by the kidneys but is toxic to the renal tubular epithelium and so may cause acute renal failure.
	en.wikipedia.org /wiki/Myoglobin (544 words)

	myoglobin. The Columbia Encyclopedia, Sixth Edition. 2001-05
		Myoglobin, which is composed of a single polypeptide chain of 153 amino acid residues, has the ability to store oxygen by binding it to an iron atom; iron is part of myoglobin’s essential chemical composition.
		Myoglobin is found abundantly in man only in cardiac muscle, which, by virtue of its essential function, must possess the capacity for continued activity when environmental oxygen concentrations are low.
		Myoglobin has been investigated intensely and is the first protein molecule to have been completely described in terms of its three-dimensional geometry.
	www.bartleby.com /65/my/myoglobi.html (267 words)

	Myoglobin - Serum - Health Encyclopedia - NBC10.com \| WCAU
		Serum myoglobin is a test that measures the amount of myoglobin in the blood.
		Myoglobin has oxygen bound to it, thus providing an extra reserve of oxygen so that the muscle can maintain a high level of activity for a longer period of time.
		Myoglobin levels may be obtained to confirm suspected muscle damage, including heart and skeletal muscle damage.
	www.nbc10.com /encyclopedia/6864730/detail.html (600 words)

	Myoglobin and Hemoglobin
		Myoglobin and hemoglobin are hemeproteins whose physiological importance is principally related to their ability to bind molecular oxygen.
		Myoglobin is a monomeric heme protein found mainly in muscle tissue where it serves as an intracellular storage site for oxygen.
		Comparison of the oxygen binding properties of myoglobin and hemoglobin illustrate the allosteric properties of hemoglobin that results from its quaternary structure and differentiate hemoglobin's oxygen binding properties from that of myoglobin.
	web.indstate.edu /thcme/mwking/hemoglobin-myoglobin.html (4119 words)

	Chapter 2 - Myoglobin
		Myoglobin, an extremely compact heme protein (MW ~ 17 800), found primarily in cardiac and red skeletal muscles, functions in the storage of oxygen and facilitates the transport of oxygen to the mitochondria for oxidative phosphorylation.
		Myoglobin is particularly abundant in diving mammals including the whale, seal, and porpoise, whose muscles are so rich, they are brown.
		Myoglobin is hailed to be the first protein to be seen at atomic resolution.
	www.phattimes.com /myoglobin/chapter2.htm (1521 words)

	Serum Myoglobin - Page 2
		Myoglobin is an oxygen-storing protein found in muscles throughout the body, including the heart.
		Myoglobin is important because it acts as a reservoir of oxygen for muscles that are working.
		Because only trace amounts of myoglobin are found in normal blood, a normal blood test result may be reported simply as “negative.” High serum myoglobin levels could mean that the heart muscle has been severely damaged from a heart attack.
	heart.healthcentersonline.com /bloodtest/serummyoglobin2.cfm (590 words)

	Myoglobin-Monobind Inc.
		Myoglobin is a protein present in the heart and other muscles.
		When a heart attack occurs Myoglobin is one of the first cardia biomarkers to rise in the blood.
		Consequently, myoglobin testing is used to help rule out a heart attack in conjunction with other markers such as troponin.
	www.monobind.com /ccc1140-myoglobin.htm (83 words)

	Calibrated Histochemistry of Myoglobin Concentration in Cardiomyocytes -- Lee-de Grott et al. 46 (9): 1077 -- Journal ...
		The amount of myoglobin in the lightpath in both cases is the same (concentrations 0.25 µM in the biochemical assay and 0.25 mM in the histochemical assay, respectively).
		The latter equation is used for the calculation of the myoglobin concentration from the absorbance in sections stained for myoglobin.
		The myoglobin concentration was determined from the absorbance measured in the section and the results shown in Figure 4.
	www.jhc.org /cgi/content/full/46/9/1077 (3427 words)

	Myoglobin: The Test
		Myoglobin levels start to rise within 2-3 hours of a heart attack or other muscle injury, reach their highest levels by about 8-12 hours, and generally fall back to normal by about one day after injury occurred.
		Myoglobin levels are often used every 2-3 hours for the first several hours after a patient who has chest pain comes to the emergency room.
		Because myoglobin is also found in other muscles, high levels usually require using other tests (such as CK–MB or troponin) to tell whether the damage was to heart or to other skeletal muscle.
	www.labtestsonline.org /understanding/analytes/myoglobin/test.html (384 words)

	Myoglobin
		Myoglobin is an oxygen-binding protein pigment found in the skeletal muscle.
		Myoglobin may occlude the structures of the kidney, causing damage such as acute tubular necrosis or kidney failure.
		Myoglobin is a single-chain protein of 153 amino acids, containing an iron porphyrin group in the center.
	www.greatvistachemicals.com /proteins-sugars-nucleotides/myoglobin.html (592 words)

	myoglobin
		The study of Myoglobin (Mb) provides a model of a weakly bound protein that reacts with 1:1 stoichiometry. The structure of Mb closely resembles that of the alpha-chains of hemoglobin, providing a system to probe without the complications of cooperativity from the 4 Hb subunits.
		Myoglobin and cytochrome b5 constitute the model system for our “dynamic docking” paradigm. The dynamic docking model decouples of the binding event from the electron transfer (ET) event.
		However, the binding event is drastically different, observed by the focusing of ‘hits’ for the Mb(dme). This represents a higher population of reactive conformers, evidenced by the observed 100-fold increase in ET rate.
	www.chem.northwestern.edu /~bmh/et_files/myoglobin.htm (121 words)

	Biochemistry of Myoglobin
		Myoglobin, the smallest of the markers, diffuses rapidly throughout the vascular system and provides the earliest indication of AMI.
		Myoglobin is the most extensively studied biomarker as an early indicator of myocardial necrosis for patients who present to the emergency department within 6 hours of the onset of symptoms.
		Myoglobin participates in aerobic metabolism in both skeletal and cardiac muscle cells, and high levels accompany various muscle traumas.
	www.dpcweb.com /medical/heartdisease/myoglobin.html (291 words)

	Recombinant Human Myoglobin - PRO-336
		Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O(2) by its heme residue, a porphyrin ring:iron ion complex.
		Myoglobin is also thought to buffer intracellular O(2) concentration when muscle activity increases and to facilitate intracellular O(2) diffusion by providing a parallel path that augments simple diffusion of dissolved O(2).
		Studies with myoglobin variants indicate that released hemin is the primary promoter of lipid oxidation in washed fish muscle.
	www.prospec.co.il /~prospec/cart/catalog/rHuMB.html (378 words)

	C:\myoglobin\template.htm
		Lyophilized myoglobin from horse skeletal muscle (Sigma) was dissolved in 0.2 M Tris/cacodylic acid buffer pH 7.0.
		Myoglobin concentrations were determined spectrophotometrically from the absorbance difference of the ferro- and ferrimyoglobin at 434 nm using a Hewlett-Packard HP8452A diode array spectrophotometer interfaced to an IBM PC AT computer.
		The variation in peak separation as a function of temperature for the heterogeneous reaction of myoglobin (Figure 60) indicates qualitatively the temperature dependence of the rate constant of the heterogeneous electron transfer reaction of myoglobin would not have a strictly linear trend.
	www.phattimes.com /myoglobin/chapter6.htm (1938 words)

	Myoglobin: an essential hemoprotein in striated muscle -- Ordway and Garry 207 (20): 3441 -- Journal of Experimental ...
		Myoglobin is expressed in Type I, 2A and 2X fibers (absent in 2B fibers).
		Note that myoglobin (green) is uniformly expressed in the cytoplasm of differentiated myotubes and absent in the nuclear compartment (propidium iodide stains red and demarcates the nuclear compartment).
		Myoglobin is important for postischemic recovery in the heart.
	jeb.biologists.org /cgi/content/full/207/20/3441 (2768 words)

	Hemoglobin and Myoglobin (page 8) (Site not responding. Last check: 2007-10-24)
		Myoglobin is a monomeric, single polypeptide strand, heme protein which is found with the muscle cells where it stores oxygen.
		Myoglobin is formed by 153 amino acids and a heme group, similar to a subunit of hemoglobin Myoglobin is 75% alpha helices.
		The hydrophobic interactions between the tetrapyrrole ring and hydrophobic amino acid R groups on the interior of the cleft in the myoglobin protein stabilize the heme protein conjugate.
	www.bergen.org /ACADEMY/Bio/molbio/AAMB5_Lesson/HEME/page_8.html (288 words)

	Imaging gas migration pathways inside myoglobin
		Representation of myoglobin, highlighting its prosthetic group, the heme (in colored licorice), which is holding on to a bound CO molecule (orange).
		1 shows the structure of a myoglobin whose buried heme is bound to a CO molecule, as caught by x-ray crystallography, despite there being no obvious CO-sized channel leading to the heme.
		2 shows the locations of the xenon binding sites in myoglobin measured from x-ray crystallography, along with those predicted from molecular dynamics simulations; in the latter case the binding sites were identified as those places in the implicit ligand maps found to be energetically most favorable for Xe.
	www.ks.uiuc.edu /Research/myoglobin-pmf (959 words)

	Renal uptake of myoglobin is mediated by the endocytic receptors megalin and cubilin -- Gburek et al. 285 (3): 451 -- ...
		Renal uptake of myoglobin is mediated by the endocytic receptors megalin and cubilin -- Gburek et al.
		The uptake of myoglobin is markedly inhibited by RAP and anti-megalin or cubilin antibodies (compare A and B, C and D, E and F).
		Endocytosis of myoglobin by megalin-expressing cells is reflected by its colocalization with megalin and cubilin at the brush border and in the apical endosomal compartment.
	ajprenal.physiology.org /cgi/content/full/285/3/F451 (3662 words)

	Oxis International Inc. - Myoglobin ELISA
		Myoglobin, a heme protein with a molecular weight of approximately 17,500 Daltons is found in both cardiac and skeletal muscle.
		The lowest detectable level of myoglobin by this assay is estimated to be 5 ng/ml.
		A clinical investigation was conducted to determine the accuracy of the BioCheck Myoglobin ELISA as compared to the Abbott AxSym Myoglobin MEIA.
	www.oxisresearch.com /product_details.html?prodid=11170 (888 words)

	A. A. Barkers Models of Myoglobin
		In 1958, John Kendrew and his team reported the first glimpse ever at the structure of a protein, that of myoglobin.
		The model they proposed gave a rough outline of the tertiary structure of myoglobin and looked somewhat like a contorted sausage out of a Daliesque nightmare.
		One particular solution was of course to produce models of the structure of myoglobin.
	www.umass.edu /molvis/francoeur/barker/barker.html (558 words)

	Cardiac markers, such as Troponins, CRP, myoglobin, GPBB, FABP, fibrinogen etc. (Site not responding. Last check: 2007-10-24)
		Myoglobin is a small hem-containing protein (153 a.a.r., MW without heme 17053 Da, theoretical pI 7,29) responsible for the oxygen deposition in muscle tissue.
		The same form of myoglobin is expressed in cardiac and in skeletal muscle tissues.
		Myoglobin appears in patients’ blood 1 — 3 hours after onset of the symptoms, reaching peak level within 8 — 12 hours.
	www.hytest.fi /high_lights5.php (1097 words)

	In vitro evolution of horse heart myoglobin to increase peroxidase activity -- Wan et al. 95 (22): 12825 -- Proceedings ...
		Myoglobin and hemoglobin are related iron protoheme IX-containing proteins that also have been studied in detail.
		Myoglobin and hemoglobin are members of the same globin superfamily and are believed to have evolved from a common ancestral
		Oxidative Modification of Tryptophan 43 in the Heme Vicinity of the F43W/H64L Myoglobin Mutant
	www.pnas.org /cgi/content/full/95/22/12825 (4789 words)

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