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At least 901 records · Page 50Linked to original sources
PubMed1995

Purification and characterization of a novel acid-soluble nuclear protein from developing embryos of the camel tick Hyalomma dromedarii (Acarina: Ixodidae).

A novel acid-soluble protein has been extracted from nuclei of developing embryos of H. dromedarii ticks and purified to homogeneity. This tick embryo basic protein (TEBP) was predominant during the cleavage stage of tick embryogenesis, whereas the complete set of histones was detectable at the late cleavage stage. The amount of TEBP reaches a maximum value at day 9 after oviposition. Thereafter, the original N-terminal dipeptide (leucine-serine) is eliminated. This coincides with the start of organogenesis. In spite of its low molecular mass, TEBP seems to be related to histone H1 in some properties such as solubility in perchloric acid and binding affinity to DNA. A task for the future will be to define the role of this protein as a counterpart of the histones for the genome organization during embryogenesis.

Amino Acid Sequence↗
PubMed1996

The sterilizing effect of pour-on flumethrin on the camel tick, Hyalomma dromedarii (Acari: Ixodidae).

The relationship between the efficacy of 1% flumethrin in pour-on formulation on the fertility of engorged female Hyalomma dromedarii and exposure time was investigated. Using a contact method, ticks were exposed in vitro to 87 micrograms active ingredient for 1, 5, 10, 30 or 720 min. Fertility inhibition was related to the exposure time. No significant effect was obtained after 1 min exposure, but 5 or 10 min exposure reduced the percentage of females ovipositing, egg mass weight, number of eggs, percentage of females laying eggs that hatch and the conversion efficiency of female weight to egg mass weight. The action of flumethrin was highly pronounced after 30 min; out of ten females, only one oviposited on the 19th day after exposure and the eggs did not hatch. Females exposed for 12 h were paralysed and showed complete sterilization. The pre-oviposition and egg incubation periods of females exposed for 1, 5 or 10 min were prolonged due to the action of the drug.

Animals↗
PubMed2004

Prostate-specific antigen immunosensing based on mixed self-assembled monolayers, camel antibodies and colloidal gold enhanced sandwich assays.

Prostate-specific antigen (PSA) is a valuable biomarker for prostate cancer screening. We developed a PSA immunoassay on a commercially available surface plasmon resonance biosensor. Our PSA receptor molecule consists of a single domain antigen-binding fragment, cAbPSA-N7, derived from dromedary heavy-chain antibodies and identified after phage display. It binds PSA with a high k(on) value of 1.9x10(6) M-1 s-1, and was covalently immobilised on a gold substrate via a mixed self-assembled monolayer (SAM) of alkanethiols by using carbodiimide-coupling chemistry in 10mM acetate buffer pH 5.5 to obtain an optimal pre-concentration. The best performing and optimised mixed SAM consisted of (10%) 16-mercapto-1-hexadecanoic acid (16-MHA) for covalent cAbPSA-N7 immobilisation and (90%) 11-mercapto-1-undecanol (11-MUOH) to minimise non-specific adsorption of the analyte. In this way, two advantages are incorporated in a single coupling layer. Up to 28 fmol/mm2 of cAbPSA-N7 could be immobilised and 30% of its binding sites participate actively in PSA interaction. In addition, the optimised layer showed also optimal performance to assess physiological samples. Although PSA concentrations as low as 10 ng/ml could be detected directly, this detection limit could be enhanced to PSA levels in the sub ng/ml range by introducing a sandwich assay involving a biotinylated secondary antibody and streptavidin modified gold nanoparticles. This approach realizes the PSA detection at clinical relevant concentrations.

Adsorption↗