Amylase Health Topic
Learn More About Amylase
Amylase on Wikipedia
Amylase is an enzyme that breaks starch down into sugar. Amylase is present in human saliva, where it begins the chemical process of digestion. The pancreas also makes amylase (alpha amylase) to hydrolyse dietary starch into di- and tri-saccharides which are converted by other enzymes to glucose to supply the body with energy.
Amylase is an enzyme produced by the exocrine glands with the ability to cleave 1,4-glucose linkages. Amylase breaks down starch into maltose and limit dextrans. The enzyme requires calcium and chloride ions for activity. Amylase is produced in the pancreas and salivary glands and to a lesser extent the fallopian tubes. From the pancreas, amylase is secreted via the pancreatic and then common bile ducts into the duodenum where it plays an important role in digestion of complex carbohydrates. In normal plasma, about 40% of circulating amylase of pancreatic origin, the rest coming from the salivary glands.
Amylase: An Enzyme That "Chews Up" Macromolecular Carbohydrate
Starch is one of nature's major energy storage compounds. Such energy storage compounds are only useful in times of need IF they can be rapidly broken down and the stored energy released. In the case of starch (aka "amylose"), there are two enzymes that do this task. Both are named amylase. It is VERY important that you notice the suffixes -ose and -ase. Enzymes usually have names that end in -ase, and things containing sugars end with -ose (such as in dextrose, sucrose and amylose). it may help you to think of enzymes as little PacMen that go around taking bites out of things. Now consider that there are two types of amylase PacMen. One has a mouth that likes to bite into the middle of the long chain of sugars that make up starch. Each bite makes a break in the chain. This PacMan is called alpha-amylase. The beta-amylase PacMan is very picky and can only "chew" on the "reducing" end of starch molecules.
Amylase Attacks hCG; and the Importance of Amylase as Precursive Enzyme Activity Before Proteinase
Graphical representation of a cancer tropoblast cell and the effect of amylase and proteases upon it. The outer coating of a cancer cell has human chorionic gonadotropin (hCG) as the suitable substrate for the attack of amylase, then protease. The proteases are unable to reach the protein until amylase does its work.
Immuno-Enzymatic Therapy: Amylase Overview (PDF File)
The first acting enzyme of the body in digestion is amylase, secreted primarily by the salivary glands and pancreas. In the mouth it begins working on carbhohydrates. Salivary amylase is known to continue acting in the upper part of the stomach before the pH drops drastically. At low pH, (acid) the enzyme is denatured, or unfolded. Calcium ions are necessary for activation of amylase. Electrolytes, chlorides and iodides increase amylase activity, while fluorides decrease it. Amylase is regularly found in the active state in plasma of the blood. Amylase is used by various white blood cells in digesting pathogens and cellular debris. Amylase can cleave the carbohydrates from hCG, deactivating it as a hormone. By cleaving the carbohydrate portions, thereby masking properties and reducing the size of the entire hCG molecule, the hCG-inhibited enzyme may be re-activated. Amylase can prevent inhibition of trypsin and the other protease enzymes by cleaving the carbohydrates away from the protein before trypsin or another protease would act on the hCG protein. Research proves that amylase can deactivate hCG, by cleaving the carbohydrate part away from the protein part. After amylase clears the carbhohydrate coating, the protein digesting enzymes can come in and digest the protein back-bone of the cell membrane, just as it does the circulating hormone.
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