Protein is di mer which has dissociated in presence of 6 M urea and it was further fragmented in 15 kd on treatment with p-mercaptoethano

Chromatography in presence of b-mercaptoethanol is most appropriate for validating the mass of nascent protein

Protein is tetramer each unit of 60 kd which fragmented into different mass peptides on vigorous treatment with urea and b-mercaptoethanol

The original 60 kd proteins made up of two 30 kd subunits associated with non-covalent interaction, when these each subunit where subsequently treated with urea and b-mercaptoethanol, a single band of 15 kd suggesting that disulphide bonds links these 30 kd subunits

A protein was purified to homogeneity. Determination of the molecular weight by molecular exclusion chromatography yields 60 kd. Chromatography in the presence of 6 M urea yields a 30-kd species. When the chromatography is repeated in the presence of 6 M urea and 10 mM b-mercaptoethanol, a single molecular species of 15 kd results. Which of the following statement is most likely to be correct?

A protein was purified to homogeneity. Determination of the molecular weight by molecular exclusion chromatography yields 60 kd. Chromatography in the presence of 6 M urea yields a 30-kd species. When the chromatography is repeated in the presence of 6 M urea and 10 mM b-mercaptoethanol, a single molecular species of 15 kd results. Which of the following statement is most likely to be correct?

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M.Sc. Entrance

CSIR NET

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