Purification and characterization of a diptericin homologue from Sarcophaga peregrina (flesh fly)
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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 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 کاملPurification and Characterization of an Inhibitor of the Cysteine Protease from the Hemolymph of Sarcophaga peregrina
The hemolymph of Sarcophaga peregrina (flesh fly) larvae was found to contain multiple inhibitors of hemocyte cysteine protease. One of them, named sarcocystatin A, was purified and found to be a mixture of the components sarcocystatin A, and AP in a molar ratio of 2:l. These components can exist in either the associated or dissociated form. The apparent heterogeneity of the protease inhibitors...
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 کاملPurification, characterization and molecular cloning of prophenoloxidases from Sarcophaga bullata.
Prophenoloxidase (PPO) is a key enzyme associated with both melanin biosynthesis and sclerotization in insects. This enzyme is involved in three physiologically important processes viz., cuticular hardening, defense reactions and wound healing in insects. It was isolated from the larval hemolymph of Sarcophaga bullata and purified by employing ammonium sulfate precipitation, Phenyl Sepharose ch...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1992
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2870573