How to identify the target protein in gel filtration and molecular sieve chromatography?

2019-04-03

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Gel filtration separates different substances based on their molecular size and is often used for desalting protein solutions. For protein solutions whose component molecules have known molecular weights, the elution time of the target protein can be estimated by comparing their molecular sizes. However, if the properties of various proteins are unknown, the only option is to collect each protein peak separately and then identify them. So, how can we estimate the elution time of the target protein simply by comparing molecular sizes? Proteins with larger molecular weights cannot enter the pores of the gel and thus have shorter elution times; conversely, proteins with smaller molecular weights can enter the gel pores and have longer elution times. Yet, this relationship is relative—for example, two large protein molecules might both fail to enter the pores at all.

　　Gel filtration separates different substances based on their molecular size and is often used for desalting protein solutions. For protein solutions whose component molecules have known molecular weights, the elution time of the target protein can be estimated by comparing their molecular sizes. However, if the properties of the various proteins are unknown, the only option is to collect each protein peak separately and then identify them individually. So, how can we estimate the elution time of the target protein simply by comparing their molecular sizes?

　　Molecules with large molecular weights cannot enter the pores of the gel and thus elute quickly; molecules with small molecular weights can enter the gel pores and therefore take longer to elute. However, this is relative—for example, if two large protein molecules both fail to enter the pores, they will elute simultaneously and cannot be separated. Therefore, gel filtration is most suitable for separating proteins with significantly different molecular weights.

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