Interaction of the mosquitocidal crystal proteins from bacillus thuringiensis isreaelensis with phospholipid vesicles
Pakistan Journal of Biochemistry. 1990; 23 (1): 13-20
in English
| IMEMR
| ID: emr-18095
ABSTRACT
The 125-130 KDa mosquitocidal proteins of the Bacillus thuringiensis israelensis delta-endotoxin were purified, activated in vitro and their interaction with phospholipid Iiposomes studied. The crystal proteins were found to cause a rapid increase in the light scattering of liposome suspensions, which reflects a morphological change in the lipid bilayer. When liposomes loaded with radioactive markers were incubated with activated crystal proteins a relatively rapid release of more than 60% of the trapped markers occurred. It is suggested that segments of the toxin molecules may become partitioned in the lipid bilayers to cause the formation of leakage pores
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Index:
IMEMR (Eastern Mediterranean)
Main subject:
Phospholipids
/
Endotoxins
/
Culicidae
Language:
English
Journal:
Pak. J. Biochem.
Year:
1990
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