Papain is a proteolytic enzyme that cleaves immunoglobulin G (IgG) into Fab and Fc fragments. On the other hand, β-mercaptoethanol is a reducing agent that breaks the disulfide bonds between the heavy and light chains of IgG. Therefore, the combination of papain and β-mercaptoethanol would result in the fragmentation of IgG into smaller fragments, including Fab and Fc fragments, as well as smaller fragments resulting from the reduction of disulfide bonds.

In terms of gel electrophoresis, the combination of papain and β-mercaptoethanol would likely result in the appearance of multiple bands of smaller molecular weight compared to intact IgG. The exact pattern of bands would depend on the specific conditions of the experiment, such as the concentration of papain and β-mercaptoethanol used, the duration of incubation, and the type of gel used for electrophoresis.

It is important to note that the combination of papain and β-mercaptoethanol may not necessarily be suitable for all experimental purposes. While it may be useful for generating specific IgG fragments, it may also result in the loss of important functional domains and may not retain the full biological activity of the intact IgG molecule.

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