...ACID HYDROLYSIS OF INTACT MYOGLOBIN Francine Nicole M. Lim, Mikko Edison P. Maniego, Lea C. Maomay, Kyle Mendoza, Meg Joen F. Misa, Sharra Jessamine Pasia ABSTRACT Myoglobin functions as an storage protein for oxygen. Hydrolysis is done primarily to obtain information about the protein. The myoglobin extracted was brownish red in color. The isolated protein was subjected to autoclaving for five hours at 15 psi. After autoclaving, the resultant solution was clear and colorless. The acid component (HCl) added prior to autoclaving was neutralized by the addition of a base, 1-molar NaOH. The neutralized acid hydrolysate was used for characterization tests and chromatography. INTRODUCTION Proteins, from the Greek proteios, meaning first, are a class of organic compounds which are present in and vital to every living cell. In the form of enzymes, hormones, antibodies, and globulins, they catalyze, regulate, and protect the body chemistry. In the form of hemoglobin, myoglobin and various lipoproteins, they effect the transport of oxygen and other substances within an organism.(1) Myoglobin is an extremely compact heme protein found primarily in cardiac and red skeletal muscles. It functions in the storage of oxygen and facilitates the transport of oxygen to the mitochondria for oxidative phosphorylation. (2) Hydrolysis is performed to obtain information about the said protein. (3) It is a process in which the compound reacts with water leading to its decomposition...
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...Chapter 4--The Three-Dimensional Structure of ProteinsChapter 4--The Three-Dimensional Structure of Proteins Student: ___________________________________________________________________________ 1. Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A. Total hydrolysis of the peptide in HCl would yield these products: A. Ala, Arg, Cys, Gln, Gly, Met B. Ala, Arg, 2 Cys, Gln, Gly, H2S C. Ala, Arg, Cys, Glu, Gly, Met, NH3 D. Ala, Arg, 2 Cys, Glu, Gly, H2S, NH3 E. None of these answers is correct. 2. Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A. The amino terminal amino acid is: A. Arg B. Cys C. Gln D. Met E. None of these. 3. Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A. The carboxyl terminal end is: A. Arg B. Cys C. Gln D. Met E. None of these. 4. Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A. The overall, net ionic charge on this peptide at pH = 7 would be: A. +2 B. +1 C. 0 D. -1 E. -2 5. The sequence of monomers in any polymer is this type of structure: A. primary structure B. secondary structure C. tertiary structure D. quaternary structure E. All of these 6. Hydrogen bonds are most important in this type of structure in proteins: A. primary structure B. secondary structure C. tertiary structure D. quaternary structure E. All of...
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...Chapter 4: Protein Function Chapter 7, Voet, Voet & Pratt * Link between protein structure and physiological function * Focus on myoglobin and hemoglobin * Both proteins reversibly bind to O2 * Extremely well-studied examples of structure/function relationships * Behavior is a model for many other proteins, especially metabolic enzymes Learning Objectives * Compare myoglobin and hemoglobin * Structures * Properties * O2 binding characteristics * Understand structural basis for hemoglobin’s O2 binding characteristics * Relate these characteristics to physiological role of hemoglobin * Understand biochemical basis of diseases/adaptations involving hemoglobin O2 Binding Proteins: Myoglobin (Mb) * Is a Monomeric protein * A single polypeptide * Has 153 residues, most are members of 8 α-helices (A-H) * Is a globular protein * Has 1 O2 binding site; reversibly binds O2 * O2: low solubility in water; diffusion through tissue is ineffective past a few mm Myoglobin Contains a Heme Prosthetic Group * Figure 7.2, 7.3 * Not responsible for knowing the structure of heme, just need to know that it contains iron which gives it is specific O2 binding properties * The color properties of this group changes due to the presence of oxygen * Red when there is oxygen is bound; blue when oxygen is not bound Myoglobin’s O2 Binding Curve is Hyperbolic * Consider the chemical equation...
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...N I N E In Cold Blood: The Tale of the Icefish In all things of nature there is something of the marvelous. -Aristotle It was a long way just to go fishing. The us-foot converted wooden sealing boat Norveg/a put to sea out of Sandcford Harbor, Norway on September 14,1927. Its primary destination was perhaps the most remote piece of land on the planet. Tiny Bouvet Island, a speck in the vast Southern Ocean, lay more than six thousand miles from Norway, sixteen hundred miles from the tip of Africa, and more than three thousand miles from South America. In the mid-1920S, commercial invention whaling was booming. The Norwegian of factory ships allowed greater numbers of animals to be taken without relying on shore facilities. Finding new stocks of whales was a priorHCllRE 9.1 The Non'egia a/ Bouvet Island. Photo (rom F;1I1gstOg Forskning r Sydish,lVct by Bjame Aagaard, Volume "N)le Tider." Published bv Cyldelldai Norsk Foriag, Oslo. 1930. ity for the entrepreneurs 2, who went to sea, and establishing tory and w.llers was a priorit) for the countries government claims to terri- involved. The Norwegian wanted to stake a claim to this icc-covered volcanic rock with 167 168 PART IV EVOLUTION IN ACT CHAPTER ON FIGURE 9.2 DitlefRlIstad 011 the Norvegia foredeck. Photo from Fangst Og Forskning I Sydishavet h)' 13,Clme i\C1gclClrd,volume "Nye Tider." Published by Cyldendal Norsk Forlag, Oslo, 1930. 9 ...
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...A Report On Malignant Hyperthermia August 2014 A Report On Malignant Hyperthermia Imagine a “hidden disease” that is usually inherited with no clear signs of symptoms until it’s suddenly triggered by drugs, or the right environmental factor or stressor. Then, once triggered, this disease induces a drastic and uncontrolled increase in skeletal muscle oxidative metabolism which overwhelms the body’s capacity to supply oxygen, regulate body temperature, and remove carbon dioxide. When this occurs, you may observe muscle rigidity, rapid heartbeat, high body temperature, muscular breakdown, and an increase in acid content (MHAUS, 2014). If not treated in a quick manner, Malignant Hyperthermia will kill. What makes this disease into a horror story is the fact that it arises upon certain triggers that are either environmental or certain types of drugs administrated from the veterinarians orders. The most common triggering agents are anesthetic gases like sevoflurane, halothane, enflurane, desflurane, and isoflurane. Certain types of muscle relaxants that are commonly added to anesthetic gases have also been known to trigger the disease as well as catecholamines, phenothiazines, and monoamine oxidase inhibitors which inhibits the activity of the monoamine oxidase enzyme family and is usually used to treat depression. That’s right! People can get Malignant Hyperthermia as well as are little furry friends. It’s not all...
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...PROTEIN FUNCTION-MYOGLOBIN AND HEMOGLOBIN 208.5.3-01-05 Hemoglobin Model Comparison to Oxygenated and Deoxygenated Hemoglobin The Bohr Effect * The Bohr effect is the relationship between hemoglobin and pH’s ability to bind oxygen. I will explain this in more detail. We begin our journey in the lungs. Our lungs have the most amount of oxygen in the body. This is a good thing because our hemoglobin is strongly attracted to and has a high affinity to oxygen. The oxygen gets heavily bound to the hemoglobin and this helps to deliver the oxygen to rest of the body. The Bohr effect allows the steady release of this bound up oxygen throughout the body while the blood is delivered to the other parts of the body such as the fingers and toes. You see our pH in the lungs is around 7.4. As the blood moves through our body our pH is changed to around 7.2 because the blood picks up carbon dioxide. Carbon dioxide is produced by our cells in the citric acid cycle and each round of the citric acid cycle causes our carbon dioxide to increase. Each cell performs this citric acid cycle, which causes a lot of carbon dioxide to build up. Our blood picks the carbon dioxide up to be able to bring it back to the lungs to be blown out of the body, but as the blood is picking up carbon dioxide it is also leaving the oxygen it needs from the blood. You see the Boher effect allows this to happen. Bohr Effect Graph Hemoglobin vs. Myoglobin Sickle Cell Anemia (amino acid) Diagram Sickle Cell Anemia...
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...A Report On Malignant Hyperthermia August 2014 A Report On Malignant Hyperthermia Imagine a “hidden disease” that is usually inherited with no clear signs of symptoms until it’s suddenly triggered by drugs, or the right environmental factor or stressor. Then, once triggered, this disease induces a drastic and uncontrolled increase in skeletal muscle oxidative metabolism which overwhelms the body’s capacity to supply oxygen, regulate body temperature, and remove carbon dioxide. When this occurs, you may observe muscle rigidity, rapid heartbeat, high body temperature, muscular breakdown, and an increase in acid content (MHAUS, 2014). If not treated in a quick manner, Malignant Hyperthermia will kill. What makes this disease into a horror story is the fact that it arises upon certain triggers that are either environmental or certain types of drugs administrated from the veterinarians orders. The most common triggering agents are anesthetic gases like sevoflurane, halothane, enflurane, desflurane, and isoflurane. Certain types of muscle relaxants that are commonly added to anesthetic gases have also been known to trigger the disease as well as catecholamines, phenothiazines, and monoamine oxidase inhibitors which inhibits the activity of the monoamine oxidase enzyme family and is usually used to treat depression. That’s right! People can get Malignant Hyperthermia as well as are little furry friends. It’s not all bad news though, Some local anesthetics have...
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...downside or health risks associated with eating red meat. People can argue that a rare or medium steak can make you sick, but I always reinforce that it depends on the way the steak is cooked and prepared. We always look for finely trimmed New York, Rib-eye or Sirloin and sear it to perfection. The nutrients, vitamins and taste of a perfectly prepared steak can and should be enjoyed by everyone, regardless of any health concerns. While red meat is generally considered to be beef, bison, venison, lamb, duck and goose due to the darker red color of the meat, I am partial to different cuts of beef. These types of meat contain myoglobin, an iron-containing protein that carries oxygen from the blood to the muscles. The higher the myoglobin levels the redder the meat. While I do enjoy a roasted or fried chicken from time to time and it does contain some myoglobin, the U.S. Department of Agriculture considers chicken, veal and pork to be white meat. 60 years ago, the beef industry changed the way they raise cattle. While cattle raised grass-fed takes 18-24 months to mature, grain/corn fed became the standard due to them reaching maturity in only 14 months. (Carol Chuang http://ezinearticles.com/?Is-Beef-Really-Bad-For-You?&id=4039733) This change not only changed the way the meat tastes, in my opinion, it changed the future of beef in general. Red meat, when prepared my way, is my primary choice in...
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...calcium levels are not normal are numbness and tingling around the mouth, muscle cramps, weakness, and bone pain. A disease process closely related to calcium is osteoporosis. Osteoporosis is the thinning of bone tissue and loss of bone density over time. It usually appears in women over 50 because of the lack of estrogen and the reabsorption of more old bone instead of new bone. These people will normally experience a fracture of the hip before they are aware of the disease. That’s why it is very crucial to include vitamin D in your diet so you can prevent these problems in the future. Iron is another mineral found in the human body. It is essential for making oxygen-carrying proteins hemoglobin and myoglobin. Hemoglobin is found in red blood cells and myoglobin is found in muscle. The best source of iron is in dried beans, liver, whole grains, and lean red meats. If one is not consuming or producing enough iron due to different disease process like leukemia, thalassemia, or poor diet...
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...The Chemistry behind a Cheeseburger The first cheeseburger was created between 1924 and 1926 by a 16 year old chef from Pasadena, California named Lionel Sternberger. The anecdote goes that a passing homeless man suggested Sternberger should add a slice of cheese to his hamburger order. Sternberger then added this to his main menu at the Rite Spot and the cheeseburger was born.1 Today the cheeseburger is marketed by not only fast food chains like Steak-N-Shake and McDonald’s but also steakhouses such as Longhorn and Logan’s Roadhouse. Whether you choose to cook your cheeseburgers at home on the grill or grab one on the go, cheeseburgers are an American tradition that everyone can enjoy. However, not all who devour this scrumptious piece of American history actually know the chemistry behind the ingredients that come together to make this delicious masterpiece. A cheeseburger would not exist without the bun to hold all of the ingredients together. The bun is made of flour, a starch or long chains of sugars molecules known as polysaccharides, yeast, salt and water. Flour, or grains are comprised mainly of wheat. When these ingredients mix, the flour gums up and absorbs all the water to produce a protein matrix called gluten. Gluten is elastic and holds the bread together to give it structure. As you knead the dough, the yeast, a living single cell creature, begins to eat the starch. When the starch is consumed by the yeast, carbon dioxide is produced. The process of microbes...
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...1 Introduction Analysis of globins allow for the evolutionary history of genes and proteins to be deduced (Goodman and Moore, 1973). A globin is a form of protein consisting of eight alpha helices (Dickerson and Geis, 1983 cited in Roesner, et al., 2004). One type of globin in-cludes the myoglobin, which functions within muscles of the heart and skeletal muscles (Hardison, 2012). The haemoglobin, on the other hand, is located within erythrocytes, and conveys oxygen from the lungs, throughout the body, and back to the lungs where it deposits carbon dioxide in exchange for oxygen (Roesner, et al., 2004). This form of protein is constructed by two alpha and two be-ta subunits, which are coded for by eight different haemoglobin genes, which in...
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...able the cell to make protons , such as collagen and elastin , which gives lots of flexibility . Lacuna is the substance that surrounding the chondrocytes. This is able to allow the collagen and elastin to form matrix. The matrix ( semi- rigid) is like an cushion that provides the strength and also has shock absorber. Cardiac muscle tissues Cardiac muscle tissues is found in the heart , it helps the heart to pump the blood around thru heart. Cardiac muscle tissues has Breached , Many Mitochondria , Intercalated discs , Myoglobin and Striated. Breached has a good flow of the electrical impulse throughout the heart. This happens because the heart muscle can contract at the same time. Many mitochondria is there to provide energy for the contraction of contractile proteins. Intercalated discs joints the cell together, so that won’t be able to separate when the muscle contracted. It also helps to transmit the electrical impulse from one cell to another. Myoglobin store oxygen to support aerobic respiration. Striated it has contractile protein that’s is lined up which is then able to create a force, that’s allow the cardiac to contract. Nerves tissues This tissues is everywhere ,But here is an example , it can be found in the brand to carry out electrical impulses. Nerves tissues has Dendron , Axon, Synaptic knob mitochondria and Schwann. Dendron has extension that links with the other neurones. It also is able to conduct impulse to the cell body. At the end of the Dendron there...
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...information (ST elevations and non ST elevations). “In transmural infarction, most infarcts are transmural involve the full thickness of ventricular wall in the distribution of single coronary artery. In Subendocardial, these infarcts involve inner one third to one half of ventricular wall, as subendocardial zone is less perfused area of myocardial zone” (Zafari, 2015). Myocardial infarction is diagnosed based on symptoms, electrocrdiographic changes, myoglobin levels, and measurement of serum CK-MB and troponins. When cell death occurs, damaged myocardial cells release enzymes into the blood stream, and these elevated enzymes can be measured in diagnostic blood tests. The enzymes are cardiac troponin T, cardiac troponin I, and a special form of creatinine phosphokinase, CK-MB. Release of these myocyte proteins in myocardial infarction is routinely used as diagnostic biomarkers. “Myocardial cell death can be recognized by the appearance in the blood of different proteins released into the circulation from the damaged myocytes: myoglobin, cardiac troponin T and I, CK, LDH, as well as many others. Myocardial infarction is diagnosed when blood levels of sensitive and specific biomarkers such as cardiac troponin or CKMB are increased in the clinical setting of acute myocardial ischaemia.” (Thygesen, Alpert, White, 2007, p. 2177) “About 25% of MI patients die before obtaining medical assistance, and 65% of MI deaths among those under age 50 occur within an hour after the initial infarction”...
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...enhance cardiac output? Baroreceptors will detect a low blood pressure and carbon monoxide levels, which would excite the sympathetic system resulting in an increased heart rate. During this mechanism the beta receptors will down regulate leaving this mechanism less effective. Prolonged stretch on the myocardium will result in myocardial hypertrophy. 3. What is the most likely cause of A.O.’s pedal edema? Right sided failure causes pedal edema. 4. What is the cause of A.O.’s exertional chest pain? What laboratory tests would be useful to confirm this diagnosis? Exertional chest pain is probably angina. Laboratory confirmation would be: * Normal CK with normal isoenzymes. * Normal troponins. * Normal myoglobin. 5. What is the rationale for the use of each of A.O.’s medications in managing her heart disease? FUROSEMIDE – loop diuretic. Activates...
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...Aldosterone: Role in Edematous Disorders, Hypertension, Chronic Renal Failure, and Metabolic Syndrome. Schrier RW, Masoumi A, Elhassan E. University of Colorado Denver, Aurora, Colorado. Abstract The role of aldosterone has expanded from the hormone's genomic effects that involve renal sodium transport to nongenomic effects that are independent of the effect of aldosterone on sodium transport. The nongenomic effects of aldosterone to increase fibrosis, collagen deposition, inflammation, and remodeling of the heart and blood vessels, however, are markedly increased in the presence of high sodium intake. The genomic effect of aldosterone increases renal sodium transport, but the administration of large doses of aldosterone to normal individuals does not cause edema, relating to the phenomenon of "aldosterone escape"; however, in edematous disorders including cardiac failure, cirrhosis, and nephrotic syndrome, impaired aldosterone escape leads to renal sodium retention and edema formation. There is now considerable evidence for the nongenomic effects of aldosterone in several important diseases. Thus, low dosages of mineralocorticoid antagonists, with little or no effect on urinary sodium excretion, have been shown to afford a beneficial effect on morbidity and mortality in patients with advanced cardiac failure and after acute myocardial infarction. Three-drug-resistant hypertension has also been found to respond to spironolactone in modest dosages. The combination of an...
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