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Antibacterial activity of a novel 26‐kDa serine protease in the yellow body of Sarcophaga peregrina (flesh fly) pupae
Author(s) -
Tsuji Yumiko,
Nakajima Yuki,
Homma Ko-ichi,
Natori Shunji
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00217-8
Subject(s) - flesh fly , serine protease , protease , flesh , antibacterial activity , pupa , biology , chemistry , botany , biochemistry , microbiology and biotechnology , horticulture , enzyme , bacteria , larva , genetics
We have reported a novel serine protease produced by Sarcophaga peregrina (Nakajima et al., J. Biol. Chem. 272 (1997) 23805–23810). This 26‐kDa protease showed antibacterial activity against several bacteria. This activity was an intrinsic characteristic of the enzyme protein and not directly related to its protease activity, because treating the 26‐kDa protease with diisopropyl fluorophosphate had no appreciable effect on its antibacterial activity. Unlike bovine trypsin, the 26‐kDa protease interacted with acidic phospholipids, suggesting that its antibacterial activity is attributable to interaction with bacterial membranes.