Fundamentals of Biochemistry: Life at the Molecular Level 5th Edition Chapter 7 - Protein Function: Myoglobin and Hemoglobin, Muscle Contraction, and Antibodies - Exercises - Page 219 17

Answer

The approximate molecular masses of an immunoglobulin G (IgG) molecule analyzed by: (i) gel-filtration chromatography: 150 kDa (ii) SDS-PAGE: 150 kDa (iii) SDS-PAGE in the presence of 2 mercaptoethanol: 50kDa and 25 kDa Explanation: Molecular mass of native immunoglobulin G (IgG) is 150 kDa. As, in gel-filtration chromatography and SDS-PAGE proteins run in their native structure, both the process will determine the molecular mass as 150 kDa. But in reducing SDS-PAGE or SDS-PAGE in the presence of 2 mercaptoethanol protein's monomers are separated. Immunoglobulin G (IgG) is a tetrameric protein which is made up of two 50 kDa subunits and two 25 kDa subunits. So, the approximate molecular masses of an immunoglobulin G in reducing SDS-PAGE or SDS-PAGE in the presence of 2 mercaptoethanol it will determine the molecular mass as 50 kDa and 25 kDa.

Work Step by Step

Update this answer!

You can help us out by revising, improving and updating this answer.

Update this answer

After you claim an answer you’ll have 24 hours to send in a draft. An editor will review the submission and either publish your submission or provide feedback.