The Massachusetts strain of avian infectious bronchitis virus was purified from embryonated hens' eggs. Four major species of apparent mol. wt. 90000, 52000, 29000 and 26000 were resolved by SDS-polyacrylamide gel electrophoresis. Omission of reducing agent failed to resolve the 29000 mol. wt. component. Labelling of acrylamide gels with I-concanavalin A indicated that polypeptides of mol. wt. 90000, 29000 and 26000 were glycosylated and, in the absence of reducing agent, that the 29000 species migrated as a dimer in the 5000 mol. wt. region. Purified IBV radio-iodinated with Bolton and Hunter reagent, which banded as a single peak of radioactivity in Metrizamide gradients, was found to contain bands of radioactivity when analysed by SDS-PAGE, corresponding to the polypeptides of mol. wt. 90000, 52000 and 29000 resolved in stained gels. Disruption of IBV particles in Triton X-100 released two subviral particles, a 16 nm spike which comprised polypeptides of 90000, 52000 and 29000 mol. wt. and another denser spherical particle of 25 to 45 nm which contained RNA and the 52000 and 26000 polypeptides.


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