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Study of kinetic parameters of LDH
BIOL2260 - Biological Chemistry
1 Found helpful • 18 Pages • Essays / Projects • Year: Pre-2021
Lactate dehydrogenase (LDH) activity exists as five different isoenzymes in mammalian tissues, each catalysing the same reaction, although exhibiting different kinetic properties depending upon their subunit composition. The amount and distribution of these enzyme forms is characteristic for a particular tissue and indeed can be a useful way of fingerprinting a tissue. Each isoenzyme is a tetramer made up of only two types of subunits: the H (heart) and M (muscle) subunits: the various combinations of which account for the five different isoenzyme forms: M4, M3H, M2H2, MH3 and H4. In this experiment, you will determine two kinetic parameters (KM and Vmax) of two different isoenzymes of LDH and relate these differences to their metabolic roles in vivo. The two isoenzymes studied will be the M4 and the H4 isoenzymes which are the predominant forms found in skeletal muscle and heart muscle respectively. In the second part of this practical class, you will examine the dependence of enzyme concentration upon rate of reaction, again using the same LDH enzyme assay system that has been used for the other exercises. Each group of students will determine the kinetic parameters of only one isoenzyme i.e. H4 or M4. Graded 19/20
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