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At least 37 records · Page 2Linked to original sources
PubMed1998

Gas chromatography with electron-capture and nitrogen-phosphorus detection in the analysis of pesticides in honey after elution from a Florisil column. Influence of the honey matrix on the quantitative results.

A modified procedure to extract pesticides from honey samples that involves loading the honey onto a Florisil packed column and subsequently eluting it with an n-hexane-dichloromethane mixture is proposed. Anomalous high gas chromatographic responses and subsequently very high recoveries for the pesticides in the extracts were obtained by a conventional calibration with pesticide solutions in organic solvent. This effect was attributed to the honey matrix and can be circumvented by using spiked honey extracts as calibration standards.

Chromatography, Gas↗
PubMed2001

Study of acaricide stability in honey. Characterization of amitraz degradation products in honey and beeswax.

A study on the possible degradation of amitraz, bromopropylate, coumaphos, chlordimeform, cymiazole, flumethrin, and tau-fluvalinate during the storage of honey was carried out by HPLC. Except amitraz, the other acaricides are stable in this medium for at least 9 months. Degradation studies of amitraz in honey and beeswax were carried out; the degradation products detected in both matrices were 2,4-dimethylphenylformamide (DMF) and N-(2,4-dimethylphenyl)-N'-methylformamidine (DPMF). The reaction rate constants and the half-lives of the amitraz degradation in honey and wax were calculated. Amitraz was nearly completely degraded within 1 day in beeswax and within 10 days in honey. When amitraz-spiked combs are recycled into new beeswax, DMF was found to be the principal degradation product left in pure wax.

Animals↗
PubMed2004

Immunochemical approach to detection of adulteration in honey: physiologically active royal jelly protein stimulating TNF-alpha release is a regular component of honey.

The presence of royal jelly (RJ) proteins in honey collected from nectars of different plants, origin, and regions and in honeybee's pollen was detected by Western-blot analysis using polyclonal antibodies raised against water-soluble RJ-proteins. The most abundant RJ-protein in honeybee products corresponded to a 55 kDa protein. The N-terminal amino acid sequence of 55 kDa protein was N-I-L-R-G-E. This sequence is identical to the apalbumin-1, the most abundant protein of RJ. Apalbumin-1 is a regular component of honeybee products and thus is a suitable marker tool for proving adulteration of honey by means of immunochemical detection. Its presence in all tested samples of honeys and honeybee pollen was confirmed also by Western-blot analysis using polyclonal antibodies raised against recombinant apalbumin-1. It has been found that major RJ-proteins, apalbumin-1, and apalbumin-2, stimulate mouse macrophages to release TNF-alpha, which demonstrates that physiologically active proteins of honey could be used for its biological valuation.

Amino Acid Sequence↗
PubMed2006

Application of Fourier transform midinfrared spectroscopy to the discrimination between Irish artisanal honey and such honey adulterated with various sugar syrups.

A collection of authentic artisanal Irish honeys (n = 580) and certain of these honeys adulterated by fully inverted beet syrup (n = 280), high-fructose corn syrup (n = 160), partial invert cane syrup (n = 120), dextrose syrup (n = 160), and beet sucrose (n = 120) was assembled. All samples were adjusted to 70 degrees Bx and scanned in the midinfrared region (800-4000 cm(-1)) by attenuated total reflectance sample accessory. By use of soft independent modeling of class analogy (SIMCA) and partial least-squares (PLS) classification, authentic honey and honey adulterated by beet sucrose, dextrose syrups, and partial invert corn syrup could be identified with correct classification rates of 96.2%, 97.5%, 95.8%, and 91.7%, respectively. This combination of spectroscopic technique and chemometric methods was not able to unambiguously detect adulteration by high-fructose corn syrup or fully inverted beet syrup.

Beta vulgaris↗
PubMed1975

Elemental analysis of honey as an indicator of pollution. Forty-seven elements in honeys produced near highway, industrial, and mining areas.

Nineteen samples of honey taken from grocery shelves, near zinc mines, adjacent to an industrial area, and near a major highway, and one sample collected in 1899 were subjected to spark source mass spectrometry to determine the concentration of most of 47 elements in the honey. Certain samples of honey produced by bees in the vicinity of the New York State Thruway appeared to contain elevated levels of certain elements known to be emitted by traffic, such as aluminum, barium, calcuim, copper, magnesium, nickel, palladium, and silicon, but the true source of these elements was uncertain. Honey that had come into contact with metal containers in processing contained the greatest amounts of zinc and tin.

Air Pollution↗
PubMed1994

Multiplication of Clostridium botulinum in dead honey-bees and bee pupae, a likely source of heavy contamination of honey.

Multiplication of Clostridium botulinum in honey-bees was examined to explain the heavy contamination of honey which may occur with this pathogen. When dead bees were inoculated with C. botulinum spores at levels of 10(2)-10(3) and incubated aerobically for 10 days, the organisms increased to 10(4)-10(5). When botulinum spores were inoculated together with Bacillus alvei, the growth of most strains was significantly enhanced (10(5)-10(7)). Similar results were obtained in bee pupae, but not in bee larvae. The heavy contamination of honey with botulinum spores that we have sometimes encountered may have been caused by contamination from dead bees in which C. botulinum had proliferated.

Animals↗
PubMed1977

Immunoassay for honey bee cytochrome c in single animals with cytochrome c-coated bacteriophages: a sensitive tool for the study of caste formation in the honey bee, Apis mellifera.

The development of a sensitive viroimmunoassay for honey bee cytochrome c and its usage for early detection of caste differentiation is described. Pure honey bee cytochrome c was isolated from workers and used to produce antibodies in rabbits. Bacteriophage T4 was chemically modified by covalent attachment of honey bee cytochrome c using tolylene-2,4-diisocyanate as a cross-linking agent. The immunospecific inactivation of this bacteriophage-cytochrome c conjugate by anti-cytochrome c antibodies can be inhibited by free cytochrome c. In quantitative determinations, 50% inhibition is reproducibly achieved at a concentration of 6 ng/ml (5 pmol/ml) and as little as 0.3 ng/ml (0.25 pmol/ml) could be detected by this system. Cytochrome c concentrations were measured in individual animals and substantial differences corresponding larval stages of worker and queen bees are reported.

Antibodies↗
PubMedDate not supplied

Multiple virus infections in the honey bee and genome divergence of honey bee viruses.

Using uniplex RT-PCR we screened honey bee colonies for the presence of several bee viruses, including black queen cell virus (BQCV), deformed wing virus (DWV), Kashmir bee virus (KBV), and sacbrood virus (SBV), and described the detection of mixed virus infections in bees from these colonies. We report for the first time that individual bees can harbor four viruses simultaneously. We also developed a multiplex RT-PCR assay for the simultaneous detection of multiple bee viruses. The feasibility and specificity of the multiplex RT-PCR assay suggests that this assay is an effective tool for simultaneous examination of mixed virus infections in bee colonies and would be useful for the diagnosis and surveillance of honey bee viral diseases in the field and laboratory. Phylogenetic analysis of putative helicase and RNA-dependent RNA polymerase (RdRp) encoded by viruses reveal that DWV and SBV fall into a same clade, whereas KBV and BQCV belong to a distinct lineage with other picorna-like viruses that infect plants, insects and vertebrates. Results from field surveys of these viruses indicate that mixed infections of BQCV, DWV, KBV, and SBV in the honey bee probably arise due to broad geographic distribution of viruses.

Amino Acid Sequence↗
PubMed1985

A double blind study on immunotherapy with chemically modified honey bee venom: monomethoxy polyethylene glycol-coupled versus crude honey bee venom.

24 patients with honey bee sting allergy were treated with either honey bee venom (HBV) or monomethoxy polyethylene glycol-coupled HBV (PEG-HBV) in a double blind trial. Both treatments induced a strong increase in HBV-specific IgG antibodies in most patients. Immunotherapy with PEG-HBV was much better tolerated than that with HBV. Conversely, patients on HBV did considerably better during a sting challenge with a living honey bee. Only 4 developed a large local and one a mild systemic reaction compared to 7 large local and 3 moderate to severe systemic reactions in the PEG-HBV-group. A higher maintenance dose of PEG-HBV may still be well tolerated but prove more effective at reexposure.

Adult↗
PubMed1986

[Proteins of bee honey. VI. Isoelectric focusing of amylase in various kinds of honey].

The isolated honey amylase was characterized by preparative and analytical isoelectric focusing. An interesting aspect of the preparative isoelectric focusing was the reduction of iodine by Ampholines which were used for building up a pH-gradient, giving a false increase in apparent amylase activity as determined by the iodine/starch reaction. Dextran gels were not suited for the matrix, because interactions with the enzyme disturb the focusing. From the analytical isoelectric focusing of isolated honey amylase in ultrathin layer Polyacrylamide gels 10 protein bands resulted. A newly developed zymogram technique was positive for amylase activity in all 10 protein bands.

Amylases↗
PubMed1977

[The proteins of honey. III. Separation of honey amylase by hydrophobic partition chromatography (author's transl)].

Previous experiments to separate the amylase and "invertase" of honey by chromatography on sephadex-gels were unsuccesful. It was shown that honey-amylase, -like amylases form other sources -- has hydrophobic properties. Therefore it was possible to separate amylase-activity from other activities by means of hydrophobic affinity chromatography on phenyl-butylamine-Sepharose 4B.

Amylases↗
PubMed2000

Optimized extraction procedure for quantifying norisoprenoids in honey and honey food products.

Norisoprenoids appear as promising compounds for authenticating unifloral honeys. So far, however, no method has been optimized for their isolation from a matrix so rich in sugars. In this framework, an original extraction procedure based on the use of Amberlite XAD-16 was developed. Recovery factors were determined and compared with those obtained with another resin (XAD-2). This was done for different model media and various norisoprenoids. In aqueous or alcoholic solutions, the efficiency of both resins proved very high. As expected, addition of honey decreased the adsorption of nonpolar compounds. This effect was much more pronounced with the lower-porosity XAD-2 support. Sugar addition markedly improved the recovery factors obtained with the XAD-16 resin in the case of more polar norisoprenoids.

Chromatography, Gas↗
PubMed2005

Making artificial honey using yeast cells from salivary glands of honey bees.

The salivary glands of a honey bee, Apis cerana and the yeast cells isolated from these glands were studied for their effects on sucrose solution. This solution exhibited lowered pH and increased levels of fructose and total amino acids as the time of incubation proceeded. The solution thus made was similar to the natural honey.

Animals↗
PubMed1983

Honey bee venom specific immunoglobulin G4 in honey bee sting allergic patients and bee keepers.

Honey bee venom (HBV) IgG4 antibody was studied in bee keepers and honey bee sting allergic patients on immunotherapy using mouse monoclonal anti-human IgG4 antibody in a modified microtiter solid phase radioimmunoassay (MSPIRA). The mean HBV IgG4 in bee keepers was 31 units/ml. In patients the mean HBV IgG4 pre- and post-immunotherapy were 2.9 and 11.6 units/ml, respectively, representing a mean rise of 7.3-fold as compared to a rise of 1.6-fold for total HBV IgG. The mean HBV IgG level in bee keepers was 14 micrograms/ml which was not significantly different from the mean level of 17 micrograms/ml in allergic patients at diagnosis. The percentage interference of HBV IgE detection in vitro correlated with HBV IgG but not with HBV IgG4. On the other hand, there was an inverse relationship between serum HBV IgE and HBV IgG4 levels while none was found for HBV IgE and IgG.

Antibodies, Anti-Idiotypic↗
PubMed1983

Antibody responses to honey-bee venom and monomethoxy-polyethylene glycol-modified honey-bee venom in mice.

Antibody responses of the IgE isotype were raised in mice with honey-bee venom (HBV) administered in alum or by daily injections without adjuvant. The sensitized mice were treated with single injections of HBV modified with monomethoxy-polyethylene glycol. By such treatment with modified but not with natural HBV, suppression of the IgE antibody responses was achieved. The IgG antibody responses, in contrast, were unchanged or enhanced.

Adjuvants, Immunologic↗