Immunoaffinity purification of juvenile hormone-binding protein from Galleria mellonella hemolymph.

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The structure of the juvenile hormone binding protein gene from Galleria mellonella.

Juvenile hormone (JH) and ecdysone are the key hormones controlling insect growth and development. The juvenile hormone binding protein (JHBP) is the first member in the array of proteins participating in JH signal transmission. In the present report a whole jhbp gene sequence (9790 bp) is described. The jhbp gene contains four introns (A-D). All the introns have common flanking sequences: GT a...

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Two disulphide bridges are present in juvenile hormone binding protein from Galleria mellonella.

The hemolymph juvenile hormone binding protein (JHBP) from Galleria mellonella contains two disulphide bridges/molecule and no free Cys residues. An alignment of primary structures of other Lepidopteran JHBPs indicates that Cys residues, equivalent to Cys10,17,151,195 in G. mellonella JHBP, maybe involved in -S-S- bridge formation.

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Purification and characterization of eight peptides from Galleria mellonella immune hemolymph.

Defense peptides play a crucial role in insect innate immunity against invading pathogens. From the hemolymph of immune-challenged greater wax moth, Galleria mellonella (Gm) larvae, eight peptides were isolated and characterized. Purified Gm peptides differ considerably in amino acid sequences, isoelectric point values and antimicrobial activity spectrum. Five of them, Gm proline-rich peptide 2...

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The effect of Galleria mellonella hemolymph polypeptides on Legionella gormanii.

Among Legionella species, which are recognized to be pathogenic for humans, L. gormanii is the second prevalent causative agent of community-acquired pneumonia after L. pneumophila. Anti-L. gormanii activity of Galleria mellonella hemolymph extract and apolipophorin III (apoLp-III) was examined. The extract and apoLp-III at the concentration 0.025 mg/ml caused 75% and 10% decrease of the bacter...

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Anti-Listeria activities of Galleria mellonella hemolymph proteins.

We report the use of antimicrobial hemolymph proteins from the model host Galleria mellonella as an inhibitor for various Listeria strains, providing a novel source for antilisterial therapeutics. We also have shown that specific virulence-associated genes known to mediate antimicrobial resistance of Listeria in mammalian models indicated a similar function in Galleria.

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ژورنال

عنوان ژورنال: Acta Biochimica Polonica

سال: 1996

ISSN: 1734-154X,0001-527X

DOI: 10.18388/abp.1996_4456