The evolution of endopeptidases—XII. The proteolytic enzymes of the honeybee (Apis Mellifica L.)

Giebel, W.; Zwilling, Robert; Pfleiderer, Gerhard

doi:10.1016/0305-0491(71)90297-5

Cited by 27 publications

(20 citation statements)

References 20 publications

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“…As other enzymes did not show this strange behaviour, we concluded that a specific interaction must have occurred between an antiserum component and the antigens studied. A similar observation of perturbed mobility in the second dimension, in work on cathodal honey-bee mid-gut endopeptidases, was reported but left unexplained (Giebel et al, 1971). As dialysis of the antiserum did not affect this mobility inversion, we concluded, after careful controls on all physical parameters, that the interference must be due to a macromolecular constituent in the serum.…”

Section: Irregular Immunoprecipitationsupporting

confidence: 82%

Subtilopeptidase A isoenzyme system. Interaction with serum components and its importance for quantitative immunoelectrophoresis

Verbruggen¹

1975

Biochemical Journal

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A method was developed which involved electroimmunoassay and crossed immunoelectrophoresis of subtilopeptidase A (EC 3.4.21.14). Initial trials with unfractionated antiserum were not successful and interaction of the enzyme with non-immunoglobulin serum components were shown to be the cause of the failures. Quantitative immunoelectrophoresis was possible when purified immunoglobulins were used. A pH of6.5 (lower than the usual pH8.6) was necessary to obtain a proper baseline definition. Subtilopeptidase A was confirmed as a multiple isoenzyme system. Qualitative inter-batch variations were detected. Di-isopropyl phosphorofluoridate inhibition altered the electrophoretic pattern, but no loss of antigenic determinants was observed.

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Section: Irregular Immunoprecipitationsupporting

confidence: 82%

Subtilopeptidase A isoenzyme system. Interaction with serum components and its importance for quantitative immunoelectrophoresis

Verbruggen¹

1975

Biochemical Journal

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“…Based on these observations, the author speculated that enzyme secretion occurred in the anterior midgut while nutrient absorption followed in the posterior regions and that the main function of the peritrophic membrane was to distribute the digestive enzymes evenly throughout the midgut. Giebel et aL (1971) (Stanley and Linskens, 1974), or microbial sources (Barker and Lehner, 1972;Gilliam et al, 1988). Grogan and Hunt (1979) analyzed proteases in pollen of 14 plant species which were frequently foraged by honey bees and found that all of the pollen samples contained chymotrypsin-like activity, but trypsin-like and carboxypeptidase-like activities were irregular.…”

Section: Introductionmentioning

confidence: 99%

Age-related changes in midgut ultrastructure and trypsin activity in the honey bee, Apis mellifera

Jimenez¹,

Gilliam²

1989

Apidologie

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Summary — Trypsin-like activity was detected in the epithelial tissue, in the fluid of the ectoperitrophic space, and within the endoperitrophic space of the midgut of adult worker honey bees, Apis mellifera. It was highest in free-flying bees and in caged bees fed pollen. Lower levels occurred in caged bees restricted to sucrose syrup or fed sucrose syrup in addition to either Beltsville Bee Diet or egg albumin. Levels of midgut trypsin activity were dependent on the amount of protein diet consumed. Both diet consumption and trypsin-like activity decreased as the bees aged. Ultrastructural changes in the midgut tissue accompanied this decline in enzymatic activity. In five-day-old pollen-feeding bees, the apical cytoplasm of cells in the posterior midgut contained numerous electronopaque vesicles, and the brush border in the crypts of the distal midgut was composed of short pleomorphic microvilli. Apical discharge from the midgut cells released the opaque vesicles into the midgut lumen. However, in 30-day-old field bees, the number of opaque vesicles and the microvesiculation of the brush border were reduced. Thus, the presence of the endogenously produced endoprotease and the regional variation in cell ultrastructure suggest that the honey bee may rely on countercurrent flow to distribute enzymes and nutrients efficiently throughout the midgut. Apis mellifera— midgut ultrastructure -enzymatic activity -trypsin -age

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“…Pavlovsky and Zarin (1922) found qualitatively no differences in the midgut enzymes between workers and drones (carbohydrases, proteases, lipase and others). But Giebel et al (1971) described clear qualitative differences within the class of proteases. In drones, as in workers, the level of proteolytic activity in the midgut corresponds to the amount of pollen present there (Szolderits and Crailsheim, 1993).…”

Section: Physiology Of Digestion In Workers and Dronesmentioning

confidence: 99%

“…Several other enzymes have also been detected, such as esterases, lipases, aminopeptidases, proteases, and glucosidases (Maurizio, 1962;Delage-Darchen et al, 1982). The proteases have been investigated in the most detail (Pavlovsky and Zarin, 1922;Giebel et al, 1971;Dahlman et al, 1978;Grogan and Hunt, 1980;1984;Moritz and Crailsheim, 1987;Crailsheim and Stolberg, 1989;Del Lama et al, 2001).…”

Section: Physiology Of Digestion In Workers and Dronesmentioning

confidence: 99%

Differences in drone and worker physiology in honeybees (Apis mellifera)

2005

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-Drones and workers have completely different roles in a honeybee colony. This is reflected in many physiological, morphological and behavioural differences. Our overview mainly focuses on aspects of diet and metabolism in larvae and adults, and on the physiology of digestion. As larvae, drones have different protein and sugar requirements than workers, and in each life stage drones and workers differ in body composition (percentages of glycogen, lipids and proteins). Like queens, drones as adults are nourished by worker-prepared food, and compared to workers their ability to digest is reduced. Mature drones fly usually only under optimal weather conditions. Their flight metabolism and resting metabolism also differ from those of workers. We discuss these differences as adaptations to the different functions of the two sexes within the colony as a superorganism.nutrition / digestion / enzymes / energy metabolism / body reserves

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The evolution of endopeptidases—XII. The proteolytic enzymes of the honeybee (Apis Mellifica L.)

Cited by 27 publications

References 20 publications

Subtilopeptidase A isoenzyme system. Interaction with serum components and its importance for quantitative immunoelectrophoresis

Subtilopeptidase A isoenzyme system. Interaction with serum components and its importance for quantitative immunoelectrophoresis

Age-related changes in midgut ultrastructure and trypsin activity in the honey bee, Apis mellifera

Differences in drone and worker physiology in honeybees (Apis mellifera)

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