When separating serum proteins by cellulose acetate electrophoresis with Veronal buffer at pH 8.6, beta globulin migrates:

• A. faster than albumin
• B. slower than gamma globulins
• C. faster than gamma globulin
• D. faster than alpha-2 globulin

Answer: (C)

In alkaline cellulose acetate electrophoresis, proteins separate mainly by their net charge at the running pH. At pH 8.6, most serum proteins carry a negative charge and migrate toward the anode, with their speed depending on the charge-to-mass ratio and size. Albumin has the strongest negative charge and is the smallest among the major proteins, so it moves the fastest. As you look from the albumin region toward the gamma region, the proteins become less highly charged or larger, and their mobility decreases. The beta globulin band sits ahead of the gamma globulin band, meaning beta migrates faster than gamma but slower than the earlier, more mobile groups like alpha-2 and albumin. Therefore, beta globulin migrates faster than gamma globulin.