Abstract
1. 1. Haemolymph protein inhibitors against a fungal protease were partially purified and their properties were compared using silkworm strains having distinct electrophoretic bands. 2. 2. Great developmental changes in the inhibitory activity and electrophoretic patterns were observed. 3. 3. Inhibitor fractions separated on a DEAE-Sephacel column corresponded to the electrophoretic bands. 4. 4. Low molecular weight inhibitors, A and F were extremely heat stable but high molecular weight inhibitors, C and D were labile. 5. 5. The inhibitor C was stable at pH 5–8 but labile under strong acidic or basic conditions, whereas F was extremely stable over a wide range of pH.
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