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# 26. You have purified fabulous enzyme that scers to decrcase anxicty during exams: Size exclusion chromatography shows that it has mass of 100 kD. You take some of ...

## Question

###### 26. You have purified fabulous enzyme that scers to decrcase anxicty during exams: Size exclusion chromatography shows that it has mass of 100 kD. You take some of the 100 kD mass protein from the size exclusion column, boil it in sodium dodecyl sulfate and perform SDS-PAGE You get two bands having molccular weights of 40 kD ard 30 kD with the 30 kD) band heing twice aS dark aS the 40 kD band.Which is the best explanation of these data?A prolease has cut your prolein into (wO fragments, restrict

26. You have purified fabulous enzyme that scers to decrcase anxicty during exams: Size exclusion chromatography shows that it has mass of 100 kD. You take some of the 100 kD mass protein from the size exclusion column, boil it in sodium dodecyl sulfate and perform SDS-PAGE You get two bands having molccular weights of 40 kD ard 30 kD with the 30 kD) band heing twice aS dark aS the 40 kD band. Which is the best explanation of these data? A prolease has cut your prolein into (wO fragments, restriction nuclease has cul our protein into [WO fragments our enzyme 1S heterodimer. It consists of two different subunits: Your enzyme is heterotrimer. It consists of three different subunits, two of which have the same mass. The data conflict and make no sense

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