Which of the following typical clinical biochemical tests make use of the increased absorbance at 340 nm by NADH?Question 4Answera.Acid phosphatase and carbohydrate deficient transferrinb.Lactate dehydrogenase and aspartate aminotransferasec.Creatine kinase and gamma glutamyl transferased.Alkaline phosphatase and aspartate aminotransferasee.Alanine aminotransferase and gamma glutamyl transferase

The answer is b. Lactate dehydrogenase and aspartate aminotransferase.

Here's why:

1. Lactate dehydrogenase (LDH) is an enzyme that helps turn sugar into energy for your cells. LDH is present in many kinds of organs and tissues throughout the body, including the liver, heart, pancreas, kidneys, skeletal muscles, lymph tissue, and blood cells. The LDH test involves measuring the amount of LDH in the blood. The reaction catalyzed by LDH involves the conversion of lactate to pyruvate, with the simultaneous oxidation of NADH to NAD+. This oxidation results in an increase in absorbance at 340 nm which can be measured.

2. Aspartate aminotransferase (AST) is an enzyme found in cells throughout the body but mostly in the heart and liver, and, to a lesser extent, in the kidneys and muscles. In healthy individuals, levels of AST in the blood are low. When liver or muscle cells are injured, they release AST into the blood. This makes AST a useful test for detecting or monitoring liver damage. The AST test involves the transamination of aspartate and α-ketoglutarate to oxaloacetate and glutamate. This reaction is coupled with the reaction catalyzed by malate dehydrogenase (MDH), which involves the conversion of oxaloacetate and NADH to malate and NAD+. The oxidation of NADH results in an increase in absorbance at 340 nm which can be measured.