Investigators decide to analyze the purity of a preparation of antibody molecules using SDS polyacrylamide-gel electrophoresis (SDS-PAGE). On Lane 1 of the gel, they load a sample of the antibody. On Lane 2, they load an antibody sample that has been treated with a reducing agent called mercaptoethanol, which breaks disulfide linkages. Following electrophoresis, they see distinct bands representing polypeptides with molecular weights of 50 kD and 25 kD in Lane 2 and only one band weighing 150 kD in Lane 1. What can the investigators conclude about their antibody based on the results of this experiment

Their antibody is composed by subunits that are conected by an S-S bond that takes place in their Cys residue. When the antibody is treated with a reducing agent, these S-S bond are reduced to S-H, thus the subunits are no longer connected to each other.

The original antibody weights 150 kD, as seen in Lane 1. And the combination of these subunits are seen in Lane 2: this means there is not only one subunit of 50 kD and one of 25 kD. Rather, these subunits are repeated in the antibody, in a way such that their combined weight add ups to 150 kD (for instance 2 subunits of 50 kD and 2 subunits of 25 kD).