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Specific antibodies were prepared against the individual subunits of the hemocyanin isolated from the tarantula Eurypelma californicum. From the antibodies, the monovalent antigen-binding fragments (Fab) were made by papain treatment. Native 37S hemocyanin was incubated with individual Fab species and the labelling of the seven subunits (a, b, c, d, e, f and g) analyzed by electron microscopy. Specific labelling patterns were found for each Fab, which allowed the allocation of specific positions to each subunit within the (4 x 6)-subunit oligomer. Along the large cleft which separates the two dodecameric half-molecules, subunits f, b, c, f are located; e forms the four corners of the 37S particle, while a is found on both sides of the small cleft which separates the two hexamers within each dodecamer, d is close to a on the outer long edges, and g close to f at the side of the particle. These results and those obtained previously by means of partial dissociation and reassembly experiments, confirm and support each other, allowing the construction of a model of the quaternary structure of Eurypelma hemocyanin.

Hemocyanins in Spiders, XVI. Subunit Topography and a Model of the Quaternary Structure of Eurypelma Hemocyanin