Question

2) (i)What does KM mean experimentally in terms of what you add in an Eppendorf tube? (ii) How does it differ from KD?

Answer 1

The KM is also known as the Michaelis constant. It is defined as the amount of substrate at which the rate of the reaction is half of the maximum rate of reaction. A low value of the Km indicates that the rate of reaction is very high that is for a very low amount of substrate , the rate of reaction reches to half value of the maximum rate of reaction and the high Km indicates the low rate of the reaction it indicates that the enzyme have less affinity for the substrate. The velocity of the reaction never reach to its maximum value as it is not thermodynamically possible for the binding of enzyme to the 100%

ii) The binding affinity of the enzyme and the substrate is measured by the KD also known as the equlibrium dissociation constant , the more KD value indicates that the two molecules have the high rate of dissociation and has the very low affinity for the association . High equillibrium dissocition constant indicates that it converted into ionic stage very easily and the lo KD value indicates that the ionising power is very poor. KD of the drug is the affinity of the molecules of the drug for the receptor. It determines drug - receptor affinity.

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