The following is an image of Coommassie Blue dye stained SDS-PAGE gel. The detai

Question

The following is an image of Coommassie Blue dye stained SDS-PAGE gel. The details of gel lanes are given below:

(one of the following links below should work and will show you the image)

http://tinypic.com/r/29bmyyx/9
http://i67.tinypic.com/29bmyyx.jpg

a) Lane 1 and 7 are low molecular weight protein standards (Phosphorylase b- 97,400, BSA-66,200, Ovalbumin-45,000, Carbonic anhydrase-31,000, Trypsin inhibitor-21,500, and Lysozyme-14,400) and lane 9 is a prestained protein standards.

b) Lane 3 and 5 are ammonium sulfate fractionated partially purified proteins from eggwhite.
c) Use Lane 7 and Lane 5 to measure protein migration (use ruler shown on right hand side) and answer questions below:
i) How many bands are in the ammonium sulfate partially purified protein? What does this tell you?
ii) You believe that band shown by an arrow is ‘Ovalbumin’. Using low MW standards migration patterns determine MW of this protein. To better explain prepare a Table (as you did in SDS-PAGE lab) and plot (Use Microsoft Excel/ any graphic program or graph paper and show the graph here) and method how did you obtain the molecular weight?

iii) Is this molecular weight necessarily the molecular weight of the functional protein? Justify your answer with proper explanation.

Explanation / Answer

(i). There are total 4 bands present in the ammonium sulfate partially purified protein. This tells us that the band present in the 5th lane is cconciding with the ovalbumin in the 1st lane.

(iii). Yes, this molecular weight is the molecular weight of the functional protein.

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