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Shkiper50 [21]
3 years ago
9

Histones are small proteins with a strong positive charge at physiological pH. They are found in the nuclei of eukaryotic cells

and package DNA into nucleosomes, the fundamental structural units of chromatin. Based only on this description, what two forms of chromatography could you use, one after the other, to separate histones from other cellular proteins? Explain your reasoning.
Biology
1 answer:
algol [13]3 years ago
4 0

Answer:

Two modes of chromatography that could be used over and over, based on characteristics of histones throughout the issue, are:

  • Size-exclusion Chromatography
  • Ion exchange chromatography

Explanation:

  • <u>Using size exclusion chromatography:</u>

A stationary step, consisting of such a polymeric material with numerous pores of various sizes. The larger proteins would travel further as the solvent system comprising the analytes flows through the paper chromatography and therefore will be separated first. That was because their greater size does not in itself allow the pores found in the polymer to get trapped. Tiny proteins such as histones, and on the other hand, can pass slowly across the process to have been eluted later.

  • <u>Using Ion exchange chromatography:</u>

As even the histone properties at biological pH are strongly positively charged, through the use of highly reactive particles as when the stationary step will allow histones to connect to themselves and now all the proteins, as well as favorable proteins that are poorly absorbed, would be eluted. Many positively charged molecules, that aren't as highly charged at around the same pH as histones, will stay throughout the stationary step, however, based on whose net charge, should flow independently of histones.

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