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The enzyme alkaline phosphatase (ALP, alkaline phenyl phosphatase, also abbreviated PhoA) is a phosphatase with the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function, but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found ...
Elevated alkaline phosphatase occurs when levels of alkaline phosphatase (ALP) exceed the reference range. This group of enzymes has a low substrate specificity and catalyzes the hydrolysis of phosphate esters in a basic environment. The major function of alkaline phosphatase is transporting chemicals across cell membranes. [1]
Alkaline phosphatase, placental type is a membrane-bound glycosylated dimeric enzyme, also referred to as the heat-stable form, that is expressed primarily in the placenta, although it is closely related to the intestinal form of the enzyme as well as to the placental-like form. [7]
Because a phosphatase enzyme catalyzes the hydrolysis of its substrate, it is a subcategory of hydrolases. [1] Phosphatase enzymes are essential to many biological functions, because phosphorylation (e.g. by protein kinases) and dephosphorylation (by phosphatases) serve diverse roles in cellular regulation and signaling. [2]
Standard liver tests for assessing liver damage include alanine aminotransferase (ALT), aspartate aminotransferase (AST), and alkaline phosphatase (ALP). Bilirubin may be used to estimate the excretory function of the liver and coagulation tests and albumin can be used to evaluate the metabolic activity of the liver. [6]
Enzymes used in ELISAs include horseradish peroxidase (HRP), alkaline phosphatase (AP) or glucose oxidase. These enzymes allow for detection often because they produce an observable color change in the presence of certain reagents. In some cases these enzymes are exposed to reagents which cause them to produce light or chemiluminescence.
Phosphoric monoester hydrolases (or phosphomonoesterases) are enzymes that catalyse the hydrolysis of O-P bonds by nucleophilic attack of phosphorus by cysteine residues or coordinated metal ions.
It is defined as the quantity of alkaline phosphatase that liberates 1 mg of phosphate ion during the first hour of incubation with a buffered substrate containing sodium β-glycerophosphate. [1] This technique was the first test to measure blood alkaline phosphatase levels, and was developed by Aaron Bodansky in the early 1930s. [2]