Facts about the brain: The brain contains around billion neurons. We have all our neurons when we are babies, but they aren't yet connected as in an adult. Further, the brain is not fully myelinated until age years.
Many of the chemical reactions, which take place in in living things are controlled by enzymes. In such cases, the enzyme is a protein in the cell which lowers the activation energy of a catalyzed reaction, which serves to increase the rate of the reaction.
Alkaline phosphatase is made throughout the body. Its function is to remove phosphate groups from nucleotides and proteins, many enzymes have their activity controlled by the addition and removal of phosphate groups.
The blood serum level of Alkaline Phosphatase is used as a marker for disease. Elevated levels five-times higher than normal are found in the blood serum of people suffering from various bone and liver diseases. Irritable bowel syndrome, germ-cell tumors and liver infections will raise serum levels of Alkaline Phosphatase to a lesser extent.
To quantify the amount of activity under different conditions. To determine the effect of enzyme and and substrate concentration upon the rate of reaction. TO analyze some of the factors that control the rate of an enzyme-catalyzed reaction Alkaline phosphatase, an enzyme, increases the rate of reaction for the conversion of p-Nitro-Phenyl Phosphate pNPP, the substrate to p-Nitrophenol pNP, product and inorganic phosphate product.
The rate of this reaction is affected by inhibitory compounds, enzyme and substrate concentration, PH and temperature. Being that the subject reaction takes place in humans as well as other living thingsit is hypothesized that the reaction contained therein, take place at or near optimal conditions.
To demonstrate the effect of substrate concentration upon the rate of the reaction catalyzed by alkaline phosphatase; B to plot the velocity of the reaction versus the substrate concentration to produce the Michaelis-Menten curve; C to plot the reciprocal of the velocity versus the reciprocal of the substrate concentration to generate the linear Lineweaver-Burk plot; and, D to determine the KM, Vmax and kcat values for alkaline phosphatase from both of these plots.
Different tissues in the body make slightly different versions of the enzyme, called isozymes. In the same manner different conditions can be used to inactivate specific isozymes of Alkaline Phosphatase, the activity of specific isozymes can be measured yielding even more diagnostic information.
However, the purpose of our experiment is not medical diagnosis but rather to test the kinetic parameters of bovine intestinal alkaline phosphatase. To do this we will use para-nitrophenyl phosphate PNPP as the substrate. This allows us to measure very small quantities of the product easily.
However, only the para-nitrophenolate ion absorbs. As the name suggests this enzyme is active at acidic pH values. Because para- nitrophenol has a pKa of about 7. This addition of KOH also denatured the enzyme, therefore we could only generate one time-point per tube. By using Alkaline Phosphatase active at high pH values we will generate the anionic form of the product directly and be able to take several time points for each well.
Materials and Methods I.is and in to a was not you i of it the be he his but for are this that by on at they with which she or from had we will have an what been one if would who has her. The activity of the mutant Alkaline Phosphatase enzyme in relation to Metabolic Acidosis Ethan Plant, BSCI, Section: Abstract: Metabolic Acidosis is a condition characterized by a lack of regulation in the acid-base balance in the blood stream; patients are also regularly shown to have low levels of the Alkaline Phosphatase enzyme%(5).
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