Abstract
Changes in the activity, elution profile on a column and electrophoretic pattern of hemolymph protease inhibitors from the silkworm, B. mori, were studied during larval-pupal and pupal-adult development. Inhibitory activity increased with development in the 5th larval stage, reached a peak at the onset of spinning and then decreased gradually. The difference between the highest and lowest points was 54.1% in the female and 72.3% in the male. An appreciable difference was observed in the elution patterns of the inhibitor on a Sephadex G-75 column in the successive stages of development. By agar gel electrophoresis, at least 3 inhibitor bands were resolved for trypsin and for .alpha.-chymotrypsin respectively. The inhibitor bands against these proteases did not correspond to each other except for a negatively moving band. There was a correspondence between the transition in intensity of inhibitor bands and the change in inhibitor activity during development. The possible significance of protease inhibitors in silkworm hemolymph was discussed.