tyrosine kinase inhibitor binds and inhibits BTK. As a result of the experiment, you are able to elute BTK from the column, but in a mixture of other tyrosine kinases. Why are tyrosine kinases other than BTK present in the eluate?

Question

Chemistry

Harold Lozano

19 March, 16:35

tyrosine kinase inhibitor binds and inhibits BTK. As a result of the experiment, you are able to elute BTK from the column, but in a mixture of other tyrosine kinases. Why are tyrosine kinases other than BTK present in the eluate?

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Answers (1)

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Faith Wells · Answer 1

Answer: It is because tyrosine kinases and BTK have similar solubilities

Explanation:

In column chromatography, components of a mixture are seperated based on their relative solubilities in two non-mixing phases.

In essence, tyrosine kinases and BTK are present in the eluate due to their similar solubility rates that arise from the similar chemical structure both possess (otherwise it would be impossible for the inhibitor meant for Tyrosine kinase to bind and also inhibits BTK)

Thus, the similar solubilities of both groups is the reason they could elute out of the column without being adsorped.