ACID CYSTEINE PROTEINASE FROM THE EGGS OF SILKMOTH, BOMBYX-MORI - TISSUE DISTRIBUTION, DEVELOPMENTAL-CHANGES AND THE SITES OF SYNTHESIS FOR THE ENZYME

Acid cysteine proteinase activities were found in the pupal ovary and hemolymph from the silkmoth, Bombyx mori. The activity in mature eggs was quite high. It increased abruptly 6 days after larval-pupal ecdysis. In the hemolymph, low activity is maintained throughout the pupal stage. These were confirmed using specific antiserum and immunoblotting. Cultured hemocytes from female pupae immediately after larval pupal ecdysis synthesized and released cysteine proteinase into the medium. Cultured ovary could also synthesize the proteinase, whereas in this case, the protein was not secreted into the medium. Translation of mRNA isolated from hemocytes and ovary directed the synthesis of the enzyme in a reticulocyte lysate cell free system, indicating that there were two major sites of synthesis for cysteine proteinase in the female pupae.