A Novel Protease in the Pupal Yellow Body of Sarcophaga peregrina (Flesh Fly)
نویسندگان
چکیده
منابع مشابه
A novel protease in the pupal yellow body of Sarcophaga peregrina (flesh fly). Its purification and cDNA cloning.
We purified a novel serine protease with a molecular mass of 26 kDa from Sarcophaga pupae. This protease appeared almost exclusively in the yellow body, an organ that develops temporarily in the pupae of dipteran insects and expands to form the adult midgut by engulfing the larval midgut. cDNA analysis revealed that this protease consists of 239 amino acid residues and has significant structura...
متن کاملA Novel Protease in the Pupal Yellow Body of Sarcophaga peregrina
We purified a novel serine protease with a molecular mass of 26 kDa from Sarcophaga pupae. This protease appeared almost exclusively in the yellow body, an organ that develops temporarily in the pupae of dipteran insects and expands to form the adult midgut by engulfing the larval midgut. cDNA analysis revealed that this protease consists of 239 amino acid residues and has significant structura...
متن کاملMendelian inheritance of pupal diapause in the flesh fly, Sarcophaga bullata.
Pupal diapause (dormancy) in the flesh fly, Sarcophaga bullata, is induced by short-day photoperiods and low temperature. In this study, the inheritance mode of diapause was investigated by crossing a nondiapausing (nd) strain of S. bullata with 2 diapausing strains having different diapause capacities. The results consistently indicated that diapause incidence is inherited in a simple Mendelia...
متن کاملMode of action of a bactericidal protein induced in the haemolymph of Sarcophaga peregrina (flesh-fly) larvae.
The mode of action of a bactericidal protein (sarcotoxin I) purified from the haemolymph of Sarcophaga peregrina (flesh-fly) larvae was studied, focusing attention on its effect on the function of the membrane of Escherichia coli. Sarcotoxin I almost completely blocked the uptakes of tetraphenylphosphonium ion and proline, which are known to be driven by a membrane potential, indicating that th...
متن کاملCharacterization of the antimicrobial peptide derived from sapecin B, an antibacterial protein of Sarcophaga peregrina (flesh fly).
Sapecin B, an antibacterial protein of Sarcophaga peregrina, was divided into four peptides. A hendecapeptide derived from its helix region was found to have comparable antibacterial activity with that of the complete protein. This peptide had a much wider spectrum of antimicrobial activity than that of sapecin B, exhibiting activity on not only Staphylococcus aureus (Gram-positive) and Escheri...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1997
ISSN: 0021-9258
DOI: 10.1074/jbc.272.38.23805