Alkaline phosphatase enzyme Essay Example | Topics and Well Written Essays - 1250 words

Alkaline phosphatase enzyme - Essay ExampleThe enzyme acts by splitting off phosphoric creating an alkaline pH.Even though the physiological function of the alkaline phosphatase enzyme is not clear it still plays a vital role in the phosphate metabolism.A ingredient known as ALPL gives instructions for making the alkaline phosphatase enzyme. The role played by alkaline phosphatase enzyme is very important. It helps in the growth and development of grind away and teeth. It is active in many another(prenominal) tissues in the body such as liver and kidneys. The enzyme plays an important role in the growth and development of castanets and teeth. It is also active in many other tissues, particularly in the liver and kidneys. This enzyme operates as a phosphatase it means that helps in removing clusters of oxygen and phosphorus atoms from other molecules. This enzyme is also important for recycling phosphate in the living cells. It is common in tissues that transport nutrients includi ng intestine and kidney.In addition to the above menti atomic number 53d function, alkaline phosphatase is one of the essential elements for the process of mineralization. In this process, minerals such as calcium and phosphorus are deposited in the developing teeth and bones. The process of mineralization is important for the formation of teeth which can endure chewing and grinding and for formation of bones that are strong and rigid.According to a research undertaken by Prof. Herbert Fleisch and Prof. Gideon Rodan in an article print under the name of In searching a bone quality marker. What about Bone Mineral Density? the biological role of alkaline phosphatase enzyme in mammals includes the followingThe first three are articulated in a tissue-specific manner. The last one is ubiquitous but is abundant in liver, bone and kidney. The gene sequence of isoenzymes of alkaline phosphatase shows that the nascent polypeptide has a short signal sequence of 17 and 21 residues of amino-ac id and at its c terminal site a aquaphobic