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yields a single band Bmercaptoethanol the ores corresponding to molecular weight

ID: 219076 • Letter: Y

Question

yields a single band Bmercaptoethanol the ores corresponding to molecular weight of 70,000 Daltons.However, in the presence of pmerca SDS PAGE shows two bands corresponding to 30,000 and 20,000 Daltons (4) 5.Molecular weight of an unspecified protein is 70,000 Dalton, SDS gel electrophoresis yi Describe the native prot type of bond that exists between the subunits. tein and mention how many subunits it has, their molecular weight and the a. You treat your protein with trypsin and ran the proteolytic cleavage on the SDS-PAGE and discovered that the SDS gel still shows only band in the absence of B mercaptoethanol(BME) but shows 4 bands in the presence of BME. How would you explain these results? b.

Explanation / Answer

5) The native protein state is three dimensional structures and it has total three subunits. Molecular Wright if one subunit is 30,000 Dalton and other two has molecular weight of 20,000 Dalton each. When it was not exposed to beta Mercaptoethanol then only one band appeared and when it was exposed to beta Mercaptoethanol two band appeared. This means that they have disulfide bond linkage between them and one two band appears as one is of 30,000 Dalton and second is thick band of two 20,000 Dalton.