Asymmetric dissociation of multiply charged proteins assemblies has been frequently reported. This phenomenon, which relies on the dissociation of one or more highly charged monomers, has been shown to provide insights into the structure and organization of large monodisperse and polydisperse assemblies. Here, the process of asymmetric dissociation is investigated using the multi-subunit protein, textilotoxin, which has unusually high structural constraints on its monomers due to multiple disulfide linkages. Initially, it is shown that, contrary to previous reports, textilotoxin is made up of 6, rather than 5 subunits. Furthermore, the hexamer exists as two isoforms, one of which is substantially more glycosylated. Gas-phase dissociation studies on the hexamers reveal the subunit stoichiometry of each isoform to be (A/B)2C2D2a and (A/B)CD2aD2b, where A and B are subunits of very similar mass and D2a, D2b refer to differentially glycosylated dimers of the D subunit. The mechanism of dissociation was unusual, as rather than one subunit being largely removed prior to sequential dissociation of a second, the process was predominantly concurrent for the two smallest subunits. Furthermore, a small proportion of the dissociated species was observed to be a noncovalently associated dimer. A comparison of dissociation pathways for two neighboring charge states of the same textilotoxin isoform demonstrates that, in agreement with previous reports, variations in quaternary structure are responsible for the distinct charge states of a protein.