Lipid-bound apoLp-III is less effective in binding to lipopolysaccharides and phosphatidylglycerol vesicles compared to the lipid-free protein
Sign Up to like & getrecommendations! Published in 2019 at "Molecular and Cellular Biochemistry"
DOI: 10.1007/s11010-019-03530-x
Abstract: Apolipophorin III (apoLp-III) is an insect apolipoprotein that is predominantly present in a lipid-free state in the hemolymph. ApoLp-III from Galleria mellonella is able to interact with membrane components of Gram-negative bacteria, as part of… read more here.
Keywords: apolp iii; iii; lipid free; protein ... See more keywords
Foam fractionation of a recombinant biosurfactant apolipoprotein.
Sign Up to like & getrecommendations! Published in 2021 at "Journal of biotechnology"
DOI: 10.1016/j.jbiotec.2021.11.004
Abstract: Locusta migratoria apolipophorin III (apoLp-III) possesses the ability to exist as a water soluble amphipathic α-helix bundle and a lipid surface seeking apolipoprotein. The intrinsic ability of apoLp-III to transform phospholipid vesicles into reconstituted discoidal… read more here.
Keywords: apolp iii; iii; foam fractionation;
Choline Supplementation Sensitizes Legionella dumoffii to Galleria mellonella Apolipophorin III
Sign Up to like & getrecommendations! Published in 2020 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms21165818
Abstract: The growth of Legionella dumoffii can be inhibited by Galleria mellonella apolipophorin III (apoLp-III) which is an insect homologue of human apolipoprotein E., and choline-cultured L. dumoffii cells are considerably more susceptible to apoLp-III than… read more here.
Keywords: apolp iii; iii; choline; microscopy ... See more keywords