/muy'euh gloh"bin, muy"euh gloh'-/, n. Biochem.
hemoglobin of muscle, weighing less and carrying more oxygen and less carbon monoxide than blood hemoglobin.
Also, myohemoglobin /muy'euh hee"meuh gloh'bin, -hem"euh-/.
[1920-25; MYO- + GLOBIN]

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      a protein found in the muscle cells of animals. It functions as an oxygen-storage unit (oxygen), providing oxygen to the working muscles. Diving mammals such as seals (seal) and whales (whale) are able to remain submerged for long periods because they have greater amounts of myoglobin in their muscles than other animals do.

      There is a close chemical similarity between myoglobin and hemoglobin, the oxygen-binding protein of red blood cells. Both proteins contain a molecular constituent called heme, which enables them to combine reversibly with oxygen. The heme group, which contains iron, imparts a red-brown colour to the proteins. The bond between oxygen and hemoglobin is more complex than that between oxygen and myoglobin and accounts for the dual ability hemoglobin has to transport oxygen as well as to store it.

      In contact with venous blood, oxygen combines more readily with myoglobin than it does with hemoglobin, favouring the transfer of oxygen from blood to muscle cells. Thus, the oxygen that the working muscle requires for the energy-producing biochemical reactions is provided.

      Myoglobin has been obtained in pure crystalline form from many sources. It has a molecular weight of 16,700, about one-fourth that of hemoglobin. Though the heme portion of all myoglobins is the same, the protein portions vary considerably between species.

      Myoglobin has been of great importance in the elucidation of protein structure. In 1962 a share of the Nobel Prize for Chemistry was awarded to John C. Kendrew (Kendrew, Sir John Cowdery) for work, utilizing the technique of X-ray diffraction, that permitted construction of a three-dimensional model of crystalline sperm-whale myoglobin.

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Universalium. 2010.

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