Abstract
A major protein was isolated from larvae of the eri-silkmoth, Samia cynthia ricini (Lepidoptera : Saturniidae), and was identified as an arylphorin based on its molecular characteristics. Samia arylphorin was a hexameric protein with a molecular weight of 470, 000 and was composed of single type of subunit with a molecular weight of 77, 000. The content of aromatic amino acids (tyrosine and phenylalanine) was 19.1%, and the overall composition of amino acids was similar to other lepidopteran arylphorins. Immunological studies revealed a homology in arylphorin structure between Samia and the mulberry silkmoth, Bombyx mori (Lepidoptera : Bombycidae). The concentration of Samia arylphorin in the haemolymph increased markedly during the final larval instar and decreased by 50% during larval-pupal transformation. The arylphorin was detected not only in the haemolymph but also in the fat body at the early pupal stage, and was reduced to trace levels in haemolymph and fat body just before adult emergence.
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