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Pragya posted an Question
September 28, 2020 • 00:21 am 30 points
  • CSIR NET
  • Life Sciences

C. exposed to an antigen immunoglobulin g was fractionated by size exclusion chromatography and it was observed to have a molecular mass of 150 kda. sds-page an

C. exposed to an antigen Immunoglobulin G was fractionated by size exclusion chromatography and it was Observed to have a molecular mass of 150 kDa. SDS-PAGE analysis under reducing conditions revealed twO bands of size 50 kDa and 25 kDa. The oligomeric status of the protein consistS of 23 d a. 3 polypeptide chains of molecular mass 50 kDa. b. 6 polypeptide chains of molecular mass 25 kDa. C. one polypeptide chain of 50 kDa and 4 polypeptides of mass 25 kDa. d. two polypeptides of 50 kDa and two of 25 kDa. IISC] in the nresence oi

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    Anup Padwal best-answer

    Go through elimination of option, Option 1 and 2 wrong because it will form only one band at reducing condition (all subunit same in molecular weight) but in question it is stated that there are two band. Option 3 wrong because total molecular weight vecones 200kd but the molecular weight of protein cannot increase.

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    Anup Padwal

    Option D at non reducing condition 1 band of 150kd at reducing 2 band of 25 and 50kd ie. 2 × 25= 50 + 2×50=100 so there is 2 homodimer linked with disulphide bonds.

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    why??

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    because the given protein is madeup of 4 poly peptide. when run in non reducing condition all four subunits are linked with disulphide bonds son only one band visible. while when reducing condition all 4 subunit seperate but out of 4, 2 are of same weight and other 2 of same. so search the option where the molecular weight do not change.

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