Overview of Lactate Dehydrogenase (LDH) Test and Clinical Significance
Learn about the quantitative determination of lactate dehydrogenase (LDH), including its types, principle, clinical significance, and testing procedure. LDH is an enzyme crucial for energy production in cells and is found in various organs and tissues. High LDH levels can indicate liver disease, heart issues, kidney problems, and more, while low levels are rare. Understand the importance of LDH testing and interpretation in diagnosing health conditions.
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Presentation Transcript
Lab2 Lactate Dehydrogenase Daheeya AlEnazi Quantitative determination of lactate dehydrogenase LDH
Why do we use it? LDH is an enzyme that helps the process of turning sugar into energy for your cells to use. it is present in many kinds of organs and tissues throughout the body, including the liver, heart, pancreas, kidneys, skeletal muscles, brain, and blood cells.
Types of LDH Isoenzymes Lactate dehydrogenase test: Types, Procedure Results#Overview1#Overview1 - Internet Explorer
principle LDH catalyses the reduction of pyruvate by NADH: Pyruvate+ NADH+ H+ LDH L-lactate+ NAD+ The rate of decrease in concentration of NADPH, measured photometircally, is proportional to the catalytic concentration of LDH present in sample.
Clinical significance When illness or injury damages your cells, LDH may be released into the bloodstream, causing the level of LDH in your blood to rise. High LDH: Liver disease, heart (MI), kidney diseae, skeletal muscle(musclur dystrophy) and erythrocytes(Anaemia) Abnormally low LDH levels occur only rarely and usually aren t harmful. Clinical diagnosis should not be made on single test result.
Procedure Mix, incubate for 1 minute. Read initial absorbance (A) of the sample, start the stopwatch And read absorbances at 1min intervals thereafter for 3 min. Calculate the difference between absorbances and the average absorbance differences per minute ( A/min)
Calculation A/min x 4925 = LDH U/L Normal Range: 120-240 U/L
