You are studying a protein, \"X.\" You decide to first purify the protein from c

Question

You are studying a protein, "X." You decide to first purify the protein from cells. The steps for purification are: Centrifuge cell lysate and collect microsomal pellet and supernatant Run sample through a gel filtration column Run sample on a cation exchanger at ph 7 Run sample on an affinity column containing 250 kD 200 kD 100 kD 70 kD 50 kD 30 kD Valine 10 kD_ The SDS-PAGE (top) and Western blot (bottom) aso »o- for the purification steps are shown. Based on 200 D these results, what can you conclude about the 100 kD cellular localization and physical properties of70*D "X?" Explain your answer. 250 kD 50 kD 30 kD-- 20 kD 10 kD

Explanation / Answer

The protein X has the following properties understood from the gel SDS-PAGE and Western blot:

1. Size of the protein is approximately of the size between 100 - 200 kDaltons.

2. The protein binds to bound fractions of valine and not unbound or free ends of valine columns.

3. The protein is seen in cation exchange late fractions and that shows they are very smaller in size and are anionic by nature.

4. They are found in late fractions of gel filterate again showing that they are smaller in size.

5. They are found in microsomal supernatant protein and so do not constitute to the microsomal mass but are probably part of the lyase. This is a very important clue to the nature of the protein origin is from the microsomal region. These microsomal proteins will be involved in cell lysis.

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