Individual proteins of known subunit molecular weight and the pyrophosphatase with a native molecular weight of 39,000 dals were denatured in a buffer containing both SDS and B-mercaptoethanol. A sample of each protein was electrophoretically separated by SDS-polyacrylamide gel electrophoresis. The marker dye migrated 12 cm. Staining the gel for protein revealed the following: Distance Migrated (cm) Protein Serum albumin catalase MW 69,000 60,000 43,000 29,000 17,000 1.6 2.2 ovalbumin carbonic anhydrase myoglobin 3.5 5.2 7.4 The pyrophosphatase migrated 6.7 cm. However, when the B-mercaptoethanol was omitted, the pyrophosphatase migrated 3.8 cm. Determine the subunits molecular weight and comment on the quaternary structure of the enzyme.
Individual proteins of known subunit molecular weight and the pyrophosphatase with a native molecular weight of 39,000 dals were denatured in a buffer containing both SDS and B-mercaptoethanol. A sample of each protein was electrophoretically separated by SDS-polyacrylamide gel electrophoresis. The marker dye migrated 12 cm. Staining the gel for protein revealed the following: Distance Migrated (cm) Protein Serum albumin catalase MW 69,000 60,000 43,000 29,000 17,000 1.6 2.2 ovalbumin carbonic anhydrase myoglobin 3.5 5.2 7.4 The pyrophosphatase migrated 6.7 cm. However, when the B-mercaptoethanol was omitted, the pyrophosphatase migrated 3.8 cm. Determine the subunits molecular weight and comment on the quaternary structure of the enzyme.
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