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 for fungal proteases and subtilisin was isolated from the silkworm hemolymph, and its amino acid sequence was determined by conventional methods. The inhibitor consisted of 55 amino acid residues and had a molecular weight of 6,100. The inhibitor included eight cysteine residues and relatively large amounts of acidic amino acids, but neither alanine, methionine nor tryptophan. The amino acid sequence of FPI-F was not homologous with those of other known protease inhibitors of microbe, plant or animal origin.
Department of Applied Biology, Kyoto Institute of Technology.
M
M
Eguchi
M
M
Itoh
K
K
Nishino
H
H
Shibata
T
T
Tanaka
K
K
Kamei-Hayashi
S
S
Hara
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000737:chemistry*; D006458:Hemolymph / Q000737:chemistry; D019476:Insect Proteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification*; D012697:Serine Endopeptidases / Q000737:chemistry
D019476:Insect Proteins; D010455:Peptides; D011506:Proteins; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; C036813:lysyl endopeptidase