AMINO-ACID-SEQUENCE OF AN INHIBITOR FROM THE SILKWORM (BOMBYX-MORI) HEMOLYMPH AGAINST FUNGAL PROTEASE

A novel protein protease inhibitor (FPI-F) which is highly specific fo r fungal proteases and subtilisin was isolated from the silkworm hemol ymph, and its amino acid sequence was determined by conventional metho ds. The inhibitor consisted of 55 amino acid residues and had a molecu lar weight of 6,100. The inhibitor included eight cysteine residues an d relatively large amounts of acidic amino acids, but neither alanine, methionine nor tryptophan. The amino acid sequence of FPI-F was not h omologous with those of other known protease inhibitors of microbe, pl ant or animal origin.