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Natural-born divers and the molecular traces of evolution
June 29, 2009An aquatic lifestyle imposes serious demands for the organism, and this is true even for the tiniest molecules that form our body. When the ancestors of present marine mammals initiated their return to the oceans, their physiology had to adapt radically to the new medium. Dr. Michael Berenbrink and his colleagues at Liverpool University have been studying how myoglobin, the molecule responsible for delivering oxygen to the muscles during locomotion, has been modified in seals and whales to help them cope with the needs of a life at sea.
The researchers have found evidence indicating that the net positive charge of this protein is increased in marine mammals compared with terrestrial relatives, and they have speculated that this may help improving the solubility of the molecule. This is important as divers may contain 10 times more myoglobin in their muscles than terrestrial animals. The team has also found a conspicuous increase of the amino acid histidine in the myoglobin of strong divers, which may allow the animal to deal better with the accumulation of lactic acid that is frequent during long dives (the same build up is the cause of the cramps we sometimes get during strenuous exercise). In order to confirm that this was indeed the result of evolutionary pressure, they went on to study the molecular sequence of myoglobin in small aquatic mammals such as beavers, muskrats and water shrews, which only dive for considerably shorter periods of time, to see if they could also find evidence for the same trend. Indeed, the net charge of the myoglobin molecule in aquatic rodents was twice as high compared to their strictly terrestrial relatives, and the trend was also verified for some semi-aquatic species of insectivores. Graduate student Scott Mirceta will be presenting these latest results at the Society of Experimental Biology Annual Meeting in Glasgow on Monday 29th June 2009.
The net electric charge of any protein is directly related to the charge of its individual amino acids, and therefore it can be predicted if the amino acid sequence is known. Dr. Berenbrink's team have determined large parts of the myoglobin sequence for four different species of insectivores, and combined it with the analysis of already published sequences from other species to reach their conclusions. They were careful to select species with close terrestrial relatives that could be used as a natural control group during the sequence comparison, so that differences at the molecular level could be safely assumed to be the product of their habitat preference. "This work will contribute to our understanding of protein solubility in general", explains Dr.Berenbrink. "It will also allow the analysis of natural selection on protein structure/function in multiple parallel cases in which a high muscle myogobin content evolved, such as in divers but also in burrowing animals that normally experience hypoxia".
Society for Experimental Biology
Society for Experimental Biology
Tracking sperm whales and jumbo squid
The sperm whale and its large prey, the jumbo squid, are among the deepest divers in the ocean, routinely reaching depths of 3,000 feet or more.
Filming an ultra-fast biological reaction essential to life
A team of scientists from the USA in collaboration with staff at the European Synchrotron Radiation Facility1 (Schotte et al) have managed to film a protein at work in unprecedented detail. The protein is the oxygen-storing molecule myoglobin, which plays a central role in the production of energy in muscles. The motion of the protein was recorded using ultra-short flashes of X-ray light from the synchrotron. The new insight in the functionality of myoglobin has led to a deeper understanding of the molecular processes associated with respiration. An article on the subject was published Friday 20 June in "Science" under the title Watching a Protein as it Functions with 150-ps Time-Resolved X-
Heart failure?
Aio! is a new Finnish diagnostic method for rapidly diagnosing an acute myocardial infarct when a patient with chest pains arrives at the hospital or consults a doctor. The diagnostic system Aio! has been developed by Innotrac Diagnostics Oy with the goal of rapidly and accurately identifying in a patient-friendly way the markers secreted into the blood in connection with a myocardial infract. On the basis of the test result, the patient suffering from a myocardial infract can immediately be directed to receive the right kind of treatment. "The key benefits of Aio! are its rapidity, reliability and convenience. We have developed dry chemistry to identify the compounds that indicate the dis
Work of Nobel-prize winning scientist Dorothy Hodgkin to be Celebrated with a Landmark Event at Oxford University
The work of the Nobel-prize winning crystallographer, Dorothy Hodgkin (1910-1994), which led to the synthesis of penicillin, vitamin B12 and insulin will be honoured by the Royal Society of Chemistry (RSC) at the University of Oxford on Monday 14 May 2001 through the designation of a National Historical Chemical Landmark. Dorothy Crowfoot Hodgkin was born in Egypt in 1910 and was educated at Oxford. She received her first degree in 1932 during which she began her research in X-ray crystallography - the use of X-ray diffraction to determine the structure of a molecule. During a long and distinguished career at Oxford University, Dorothy Hodgkin elucidated the structures of the antibiotic pe
More Myoglobin Current Events and Myoglobin News Articles
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Science, 29 March 1963, Articles on Myoglobin and the Structure of Proteins, Mosquitoes Comparative Serology, Yttrium-88, Origin of Tektites, Bohr Effect, Indium Antimonide, and Much More! by American Association for the Advancement of Science. (Author) | |
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J&j Myoglobin Tests 100/bx - Model 6801042 by Johnson and Johnson J&J Myoglobin Tests 100/Bx - Model 6801042 : This product is being shipped directly to you from the manufacturer, and as such, may incur seperate delivery fees, plus freight charges. Please allow 4-6 weeks for delivery. SPECIAL NOTE: All special ordered items are "NON-RETURNABLE" Due to manufacturer no return policy this item is not returnable. Product is being shipped to you directly from the manufacturer. |
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CK-MB Myoglobin Troponin I Cardiac Status Controls () by Spectral Diagnostics Inc. These simple, handheld cardiac marker bedside tests quickly and accurately determine elevations of multiple cardiac markers, enabling health-care providers to easily assess and diagnose chest pain at the decision point. Tests feature internal controls and require no instrumentation. They can accommodate either heparinized whole blood, plasma or serum as a sample. Tests are stable when stored at room temperature. |
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Allele frequencies of single nucleotide polymorphisms in the second exon of the myoglobin gene among the Japanese. (Brief Communication).(Brief Article)(Statistical ... Included): An article from: Human Biology by Tomoyo Takata (Author), Satoru Miyaishi (Author), Yuji Yamamoto (Author), Sachiyo Inagaki (Author), Kei Yoshitome (Author), Takaki Ishikawa (Author), Hideo Ishizu (Author) This digital document is an article from Human Biology, published by Wayne State University Press on April 1, 2002. The length of the article is 863 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available in your Amazon.com Digital Locker immediately after purchase. You can view it with any web browser. From the author: KEY WORDS: SINGLE NUCLEOTIDE POLYMORPHISM (SNP), MYOGLOBIN, JAPANESE POPULATION Citation Details Title: Allele frequencies of single nucleotide polymorphisms in the second exon of the myoglobin gene among the Japanese. (Brief Communication).(Brief Article)(Statistical Data Included) Author: Tomoyo Takata Publication: Human Biology (Refereed) Date: April 1,... | |
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Alfa Vitamins Iron 136 mg 60 caps Vitality Stamina Fight Anemia by Alfa Vitamins Iron is a metal which is necessary for most forms of life as well as for normal human physiology. It forms part of many proteins and enzymes that maintain a healthy body. Iron is an essential element for life and is responsible for the vitality and stamina of our body. Iron in the human body has very important functions. Iron binds with hemoglobin, the protein in red blood cells that carries oxygen from the lungs to the rest of the body. Smaller amounts of Iron are found in myoglobin, a protein that helps supply oxygen to muscles. Cells that fight infection depend on adequate stores of Iron. This means if your Iron stores are low, your body is more prone to infections. Iron is essential in the chemical reactions that produce energy from food. Therefore, if your Iron levels are low, your... |
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Myoglobin Test: An entry from Gale's Gale Encyclopedia of Medicine, 3rd ed. by Nancy Nordenson (Author) This digital document is an article from Gale Encyclopedia of Medicine, 3rd ed., brought to you by Gale®, a part of Cengage Learning, a world leader in e-research and educational publishing for libraries, schools and businesses. The length of the article is 581 words. The article is delivered in HTML format and is available in your Amazon.com Digital Locker immediately after purchase. You can view it with any web browser. The third edition of this authoritative, comprehensive, in-depth medical guide features information on medical topics in language accessible to adult laypersons. Disease/disorder articles typically cover definition; description; causes and symptoms; diagnosis; treatments; prevention; and more. Test/treatment articles typically cover definition; purposes;... | |
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Lifesign Myoglobin/troponini/ck-mb 20tests 1/bx - Model 60201 by Lifesign Lifesign Myoglobin/TroponinI/CK-MB 20Tests 1/Bx - Model 60201 : |
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Atlas of Molecular Structures in Biology: Volume 2. Haemoglobin and Myoglobin by G. Fermi (Author) | |
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The Mathematics of Oxygen and Substrate Diffusion: Mathematical Analysis of Oxygen, Myoglobin-Facilitated Oxygen and Substrate Diffusion within an Interacting Multi-capillary System in Skeletal Muscle by Miranda Teboh-Ewungkem (Author) A theoretical model for oxygen and substrate transport to tissues within skeletal muscle involving several interacting capillaries has been developed. It involves an elegant technique that discretizes the transport problem in a tissue with large number of capillaries. The technique can be equally applied to other heat transport problems with actual anatomical information. For oxygen, the role of myoglobin and the effect of axial diffusion have been considered. For the myoglobin model, myoglobin facilitates oxygen diffusion into tissue and can prevent hypoxia due to the interaction of the capillaries. The analysis yields a great deal of information about hypoxia, since as shown, a multicapillary model of the type presented here is needed to determine if the tissue is... |
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Myoglobin. Colloquium on Myoglobin, Brussels, 22nd May 1976, Université Libre d Bruxelles. by A G Schneck (Author) |
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