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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Ashutosh
explain sir
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Anup Padwal
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...
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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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Pragya
why??
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Pragya
please explain
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