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At least 865 records · Page 48Linked to original sources
PubMed1982

Catecholamines in honey bee (Apis mellifera L.) and various vespid (Hymenoptera) venoms.

Liquid chromatography with electrochemical detection was used to separate, identify and quantitate the levels of dopamine (DA) and noradrenaline (NA) present in the venoms of honey bees of known ages and of DA and 5-hydroxytryptamine (5-HT) in various species of vespid wasps. Fluorescence histochemistry corroborated the presence of amines in honey bee venom glands and reservoirs and supported the quantitative results. The results show: (i) There is an age dependent variation in DA and NA levels in honey bee venom and there may be a similar variation in DA and 5-HT in the venom of queen Dolichovespula arenaria. (ii) There appears to be a seasonal variation in the quantities of DA and NA present in honey bee venom. Such a seasonal variation may be one of the factors involved in the variation in the levels of amine components present in the various vespid wasp venom samples. (iii) 5-HT is present in much greater quantities than DA in vespid venoms. Low levels of NA and DOPA are present in vespid venoms.

Age Factors↗
PubMed1986

Immunological effects of honey bee (Apis mellifera) venom using BALB/c mice.

Honey bee venom at concentrations up to 50 micrograms/ml was not toxic in vitro for unstimulated murine splenic lymphocytes, as assayed by tritiated thymidine incorporation. However, venom concentrations greater than 6 micrograms/ml significantly (P less than 0.01) inhibited concanavalin A (con A) simulation of murine lymphocytes. In contrast to this finding, the splenic lymphocytes from mice receiving 4 s.c. injections of honey been venom on alternate days were significantly (P less than 0.01) enhanced in their proliferative response to con A compared to a sham-injected group of mice. Mice injected with the venom prior to and following an injection of sheep red blood cells produced significantly more direct IgM plaques (P less than 0.02) than the sham-injected group. In this study both suppression and enhancement of immune reactivity was seen using honey bee venom when assayed on the splenic lymphocytes of BALB/c mice.

Animals↗
PubMed1987

The purification of acid phosphatase from honey bee venom (Apis mellifica).

Acid phosphatase from bee venom was purified by a combination of saturated ammonium sulphate precipitation, gel filtration and ion exchange chromatography. The final product which is a glycoprotein contained less than 0.1% phospholipase A2 or hyaluronidase activity and existed in two molecular weight (96,000 and 45,000) forms. Acid phosphatase is a potent allergen, in bee venom allergic patients, which is capable of releasing histamine from sensitized human basophils and of inducing a wheal and flare reactions in sensitized human skin.

Acid Phosphatase↗
PubMed1989

High resolution of honey bee (Apis mellifera) venom peptides by propionic acid/urea polyacrylamide gel electrophoresis after ethanol precipitation.

A new and simple gel electrophoretic method is described which enables the protein and polypeptide components of bee venom to be resolved on a single gel. The electrophoretic method allows octapeptides to be resolved and species as small as decapeptides can be detected at high sensitivity using the Coomassie blue staining method without prior fixation. This has been achieved by replacing acetic acid by propionic acid in acid/urea polyacrylamide gels and by controlling the amount of TEMED catalyst for the polymerisation of high concentration gels in order to obtain a low effective pore size. We demonstrated the value of ethanol precipitation as a rapid and efficient desalting the fractionation technique and propose that it could be used in combination with gel filtration to purify many of the peptides to homogeneity.

Animals↗