The hemolymph of metamorphosing, final instar larvae of Trichoplusia ni was analyzed for the presence of basic forms of normally positively charged storage proteins. Basic forms of arylphorin and a normally acidic juvenile hormone suppressible protein were identified. For each of these two proteins, variation was observed in the immunoreactivity of forms with different basic charges, where the antisera had been generated against acidic forms of each protein. A basic protein of high molecular size (ca. M(r) 150,000) was identified that cross-reacted specifically with an antiserum raised against a normally basic, M(r) 74,000 juvenile hormone suppressible protein in the hemocyanin superfamily.

The 33,000 Dalton venom protein of Chelonus near curvimaculatus was characterized for structural properties of charge, quaternary associations, and relationship to polydnavirus encoded proteins. Homogenous isoforms of the protein were isolated from the venom by sequential steps of 1) microdissection, 2) separation based on charge (Mono-Q column HPLC or narrow-range electrofocusing), and 3) centrifugal filtration based on molecular weight using Centricon microconcentrators. The purified protein dimerized under native conditions, and this quaternary association became denaturation resistant under certain conditions. Chemical modification of lysine epsilon amino groups did not disrupt such dimerization. The cDNA for the protein did not possess high similarity to any sequence encoded in the polydnavirus, as indicated by results of Southern blotting, but does possess similarity in its repeats to the repeats of the immunologically protective surface glycoprotein of Leishmania amazonensis.