Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrina (flesh fly).
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چکیده
منابع مشابه
Characterization 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 کاملIonophore activity of sarcotoxin I, a bactericidal protein of Sarcophaga peregrina.
When Escherichia coli was treated with sarcotoxin I, a potent bactericidal protein of Sarcophaga peregrina (fleshfly), K+ inside of the cells leaked out rapidly and the ATP pool of the cells rapidly decreased. These results suggested that the bactericidal effect of sarcotoxin I was due to its ionophore activity, and that it blocked the generation of ATP by inhibiting formation of the proton gra...
متن کاملPurification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina.
Three antibacterial proteins were purified from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly). Sequencing studies showed that two of these proteins belong to the sarcotoxin I family, potent antibacterial proteins purified from the hemolymph of Sarcophaga larvae, whereas the other protein, named sapecin, is a new protein consisting of 40 amino acid ...
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 کاملA 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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)75688-9