Determination of Serum Lactic Dehydrogenase Activity - Essay Example

The reason for this is because each isoenzyme contains a multiple of either H subunit or M subunit. LDH-1 contains 4 H subunits; LDH-2 has 3 H subunits and 1 M subunit etc. For this reason they are equally spaced. As each M subunit is added the isoenzyme gets heavier by a certain molecular weight. So when one M subunit is added to the isoenzyme, it gets heavier by a molecular weight of X. When another M subunit is added, it gets heavier by 2X and so on till it contains four M subunits (LDH-5).

We can use electrophoresis for diagnosis by comparing the intensities of colors produced. We can do an electrophoresis with a normal person’s serum and note the intensities of the color produced. Then we can do an electrophoresis with a patient’s serum and note the intensities of color produced. Then we can see if the intensity of color a particular LDH isoenzyme is greater than that of the normal person’s. If this is the case then we can confirm a diagnosis. LDH-1 is found in high amounts in the heart and LDH-5 is found in high amounts in the liver.

The heart muscle is continuously contracting and relaxing and hence the energy requirement for them is quite high. In order to replenish the energy supply, (NAD) in the presence of low levels of oxygen, LDH converts pyruvate to lactate. NADH is oxidized which provides the necessary energy. On the other hand, the liver cells are relatively sedentary and thus have lower energy