After running a SDS-PAGE assay on an unknown protein with molecular size 180 kD, you find that the protein shows up as two bands on the polyacrylamide gel which correlate with a 30 kD subunit and a 50 kD subunit. What is a possible ratio of 30 kD subunits to 50 kD subunits that could constitute this mystery protein?

Question

Biology

Madden Horton

22 November, 22:15

After running a SDS-PAGE assay on an unknown protein with molecular size 180 kD, you find that the protein shows up as two bands on the polyacrylamide gel which correlate with a 30 kD subunit and a 50 kD subunit. What is a possible ratio of 30 kD subunits to 50 kD subunits that could constitute this mystery protein?

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Answers (1)

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Sharon Macdonald · Answer 1

One 30 kD subunit: Three 50 kD subunits

Explanation:

SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) is a variant of electrophoresis, which is used in the analysis of molecules (proteins) on the basis os size.

Sodium dodecyl sulfate (SDS) is an ionic detergent that denatures proteins and make them uniformly charged.

In this process proteins are separated on the basis of size, not on the basis of charge, and recognized by band size.

After running a SDS-PAGE assay on an unknown protein with molecular size 180 kD proteins show two bands on the basis of size, these are of 30 kD subunit, and three 50 kD subunits,