Literature value of km for alkaline phosphatase. An investigation into the determination of Km and Vmax values for Alkaline Phosphatase 2022-12-23
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Alkaline phosphatase
Fusce dui lectus, congue vel laoreet ac, dictum vitae odio. The test tube was then removed from the water bath and the contents transferred to a curvette, using a pipette to maintain accuracy. This, in combination with V max , which represents the maximum velocity of the rate of reaction, can be used to identify between isoenzymes as each isoenzyme displays different kinetic characteristics. Using the values of K m and V max obtained, various isoenzymes of alkaline phosphatase can be distinguished between. Pellentesque dapibus efficitur laoreet. The reduced protein binding capacity can lead to a higher potential to drug-drug interactions Ginsberg et al, 2005. If Na 2HPO 4 acts as a competitive inhibitor, use your data to determine its K i value.
METHOD The only change to the method was that the concentration of the substrate altered within each experiment. Figure 1 demonstrates how the presence of phosphate effectively lowers the velocity of alkaline phosphatase. When in reciprocal form the substrate concentrations would be roughly equally separated on the x-axis, aiding in the drawing of a line of best fit which would be required in order to obtain the values of K m and V max. Values of K m and V max were then subsequently obtained through simple algebra. To determine the effects of enzyme concentration on reaction kinetics, you will be measuring the rate of enzyme catalyzed reactions at a constant concentration of substrate 0.
[Solved] what is the literature km, vmax, and ki value of alkaline...
Fusce dui lectus, congue vel laoreet ac, dictum vitae odio. Clinical Chemistry: Laboratory Management and Clinical Correlations, 1 st edn. Secondly, the solution contained only the borate buffer, pNPP, phosphate, and alkaline phosphatase. Nam risus ante, dapibus a molestie consequat, ultrices ac magna. Keep the substrate on ice until your ready to place it in the spectrophotometer. Therefore, using simple algebra, K m was calculated to be 1. Lorem ipsum dolor sit amet, consectetur adipiscing elit.
Some of the reagents found in the Nepalese market are that of Accurex, Tulip, Erba, Human, Diasys, Analyticon, etc. The relationship between rate of reaction and concentration of substrate depends on the affinity of the enzyme for its substrate. MAIN EXPERIMENT ALTERATIONS AND CHANGES The experiment methodology remained as before, however more precision was sought when measuring the 0 second reading from the spectrophotometer, as this would heavily influence the values obtained for the initial rate of reaction. Moreover the patient has not suffered from abdominal pain but has noticed the development of jaundice, which is a clear indicator of liver cirrhosis. Finally, when you get the result, multiply the value with the dilution factor 1+y.
An investigation into the determination of Km and Vmax values for Alkaline Phosphatase
Inhibition by Phosphate Derivatives and the Substrate Specificity. Whereas lowered levels, hypophosphatasemia, are associated with conditions such as hypothyroidism and malnutrition. Further, the NMR and mass spectrum provide information about the presence of a benzene ring and the corresponding fragments of the compound. This will allow you to determine the rate of substrate hydrolysis due to the enzyme alone. Student 1: With the clean pipet tip, add 60 µL of 0.
This was incubated in a 30 0 C water bath for 5 minutes, which was timed using a stop clock. Annales de Biologie Clinique. Any variation in the value of ALP can mostly be an indication of liver and bone-related diseases. A higher Km value coincides with the presence of phosphate in the solution. It must however be noted that some errors may have entered the investigation, although these are likely to be minimal and not have a major impact on the values of K m and V max obtained. The value of K m is a measure of the affinity of an enzyme for its substance.
Therefore it can be used to identify between alkaline phosphates from osteoblasts and the biliary tract. The literature value of Ki for phosphate inhibitor was found to be 438200M. Nam lacinia pulvinar tortor nec facilisis. Adjust the temperature on the Shimadzu spectrophotometer to 20. Moreover the patient has described nausea after digesting a fatty meal, a typical symptom of gallstone. The inhibitory effect of phosphate prevents the enzyme from binding to pNPP which effectively increases the experimental value of Km, which agrees with what is stated in the literature.
Enzyme Kinetics and Inhibition of Alkaline Phosphatase
It was decided that five separate enzyme concentrations would be used as this would generate enough initial rates of reaction to be able to plot a Lineweaver-Burk plot accurately. Figure 1 demonstrates that the presence of phosphate dramatically 3 decreases the velocity of the enzyme. This is because in conditions associated with the liver, all three levels increase and ALT increases relatively in order to indicate precisely what disease is present. This is because the most heat stable Mycobacterium paratuberculosis, is destroyed by temperatures lower than those required to denature the enzyme. Nam lacinia pulvinar tortor nec facilisis. These various isoenzymes exhibit different kinetic parameters, such as K m and V max values, and this can therefore be used to distinguish between them. Here are some of the diseases which can cause a decrease in the ALP level.
Nam lacinia pulvinar tortor nec facilisis. At low substrate concentrations, the catalytic site of the enzyme is empty and is waiting for the substrate to bind. Plot the data for reactions done at each enzyme concentration on the same graph. Also a pancreatic tumour can be ruled out because the patient has indicated that they have had recurrent abdominal pain for a period of a year, however no substantial weight loss has been noted. Place 4 cuvettes in the first 4 sample positions and 1 cuvette in the reference position.
