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you have an 45kD histidine tagged bacterial protein (100% pure). you apply this pure protein to a Ni+2-agarose column. then you apply a crude mouse cell extract to the column. after extensive washing, you apply an imidazole buffer. analysis of the resultant elution on an SDS-PAGE gel indicated two proteins (45kD and 90kD) of equal coomassie blue staining.

What is the simplest explanation of why the 45kD and the 90kD proteins copurified the column?

What would be an alternative explanation?

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