into muscle cells and analyze for presence of myosin light chain. Utilizing Western Blotting techniques and using specific antibodies helped to detect myosin light chain. The hypothesis was that proliferating myoblasts could be induced to initiate the differentiation process by depriving the cells of the necessary growth factors and that the differentiation is characterized by the expression of muscle-specific proteins. The results showed that that myosin light chain was not present. It was concluded
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William Perez Cell Biology 2440 Lab on protein Myosin Proteins are chains of amino acids that perform the most important functions in living organism. Every protein will contain an amino group‚ carboxyl group‚ a different R group and an alpha carbon with two hydrogens. There are nine types of functions proteins can have‚ enzymes‚ motor‚ receptor‚ structural‚ storage‚ transport‚ signaling‚ and special purpose proteins(antibodies). There are four levels of protein structure‚ primary‚ secondary
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Biochemistry of Muscle Contraction Fred P. Guillergan M.D.‚ FPCP Outline histology and biochemistry of muscles (Striated & smooth) – Myosin – Actin‚ Tropomyosin‚ Troponin – Accessory proteins of muscles Biochemical events in muscle contraction Calcium‚ Ca2+-binding proteins and Ca2+ channels in muscle contraction Biochemistry of Cardiac & Smooth muscle contraction Energetics of muscle contraction ☻Able to understand the normal anatomy and physiology of different types of muscles
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Chapter 9: Muscular System: Histology and Physiology Multiple Choice 1. The capacity of a muscle cell to shorten forcefully is known as A) contractility. B) excitability. C) extensibility. D) elasticity. E) flexibility. Answer: a Level: 1 2. Muscles exhibit the property of excitability. This means that the muscle A) shortens its length. B) recoils to its original resting length. C) stretches beyond its normal length. D) responds to stimulation by the nervous system. E)
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Sarcomere- smallest contractile element of muscle fiber‚ extends from z-line to z-line Myofilament- responsible for contraction Striated- the color variations on the muscle fiber. Has to do with the amount of protein and the way it reflects light. Myosin- globular protein Bulb like heads come in contact with the active sites on actin Active sites are not exposed when in the resting position. Tropomysin- the regulatory protein the hides the active sites when not stimulated Sarcoplasmic reticulum-
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body. Myosin and Actin is an interaction protein to Muscle Contraction‚ it can be changed by shape but not by volume. Skeletal Muscle contraction is produce by heat. The muscles may receive signal from the brain. Once it receives signal it expands or contracts. Skeleton can provide muscle movement and frame work. This kind of muscle can be found attached your bones. Filaments there are only two types of sliding filaments. The Thick Filaments is called “Myofliaments”. Myofliaments produces myosin. Myosin
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Animals have three types of muscles; skeletal‚ smooth‚ and cardiac. This lab however is only concerned with skeletal muscle. A special characteristic of skeletal muscle is their ability to contract or shorten via thin (actin) and thick (myosin) filaments (Flanagan‚2017). This gives a striated appearance which is a key distinguishing characteristic between other types of muscle (Flanagan‚2017). Skeletal muscle is also multinucleated. Skeletal muscle needs plentiful amounts of energy to be able to
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Introduction Muscle tissue is composed of as many as 19 different proteins; the largest components are myosin and actin. All muscle tissue contains actin and myosin; these form the fibers that slide past each other as muscles contract and relax. There are also a number of other proteins found in muscle tissue; these other proteins regulate movement‚ bundle and anchor actin and myosin along with others functions. As species have evolved‚ they have diverged in the quantities and types of these
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Filament theory 1. ATP binds to myosin (45°). This causes an affinity change‚ and myosin is released from actin. 2. ATP ADP + Pi and myosin heads are cocked to 90° 3. Myosin heads bind to actin to form a cross-bridge 4. Pi released‚ and myosin springs back to 45°. Actin is pulled over myosin and toward the center of the sarcomere. This causes shortening of the sarcomere and is referred to as the “power stroke” 5. ADP is released‚ but myosin remains bound to actin (rigor state)
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________ 1. Myosin heads bind to active sites on actin molecules ________ 2. ATP is hydrolyzed. ________ 3. Myosin heads return to their cocked position ready for the next working stroke. ___1____ 4. Calcium ions bind to troponin. ________ 5. Cycling continues until calcium ions return to the SR. ________ 6. Myosin cross bridges detach from actin. ________ 7. Troponin changes shape. ________ 8. ADP and inorganic phosphate are released from the thick filament. ________ 9. Myosin heads pull
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