A family of major royal jelly proteins of the honeybee Apis mellifera L.

Schmitzová, Jana; Klaudiny, Jaroslav; Albert, Štefan; Schröder, Werner; Schreckengost, William E.; Hanes, Jozef; Judova, Jana; Šimúth, Jozef

doi:10.1007/s000180050229

Cited by 284 publications

(374 citation statements)

References 48 publications

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“…Other authors also found differences (HAYDAK, 1970;PALMA, 1992;SCHMIDT;BUCHMANN, 1992;LERCKER et al, 1993;SCHMITZOVA et al, 1998;PARFITT, 1999;GARCIA-AMOEDO;ALMEIDA-MURADIAN, 2007) and attributed these differences to the nutritional status of the evaluated colonies, age of mother queens, and the laboratory methods used to analyze their components. Queiroz, Barbosa and Azevedo (2001) reported that supplementation is good, mainly in the Northeast region of Brazil, for royal jelly production throughout the year, including autumn and winter, periods between flowering, in regions of monoculture such as sugarcane plantation, limited pollen flow or low nutritional pollen quality.…”

Section: Physicochemical Quality Of Royal Jelly Samplesmentioning

confidence: 97%

Quality of royal jelly produced by Africanized honeybees fed a supplemented diet

Sereia

Toledo

2013

Food Sci. Technol

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Section: Physicochemical Quality Of Royal Jelly Samplesmentioning

confidence: 97%

Quality of royal jelly produced by Africanized honeybees fed a supplemented diet

Sereia

Toledo

2013

Food Sci. Technol

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“…some similarity with the major royal jelly protein from the honeybees [20][21][22], and several yellow-like proteins from other insects [23,24]. Recent studies suggest that the temporal and spatial profiles of Drosophila yellow-y and ebony gene together determine the pattern and intensity of melanization [25], but the mechanism by which the yellow-y gene promotes the formation of pigments is poorly understood.…”

Section: Figure 1 Sequence Alignment Of Drosophila Yellow-f Yellow-fmentioning

confidence: 99%

Identification of Drosophila melanogaster yellow-f and yellow-f2 proteins as dopachrome-conversion enzymes

Han

Fang

Ding

et al. 2002

Biochemical Journal

143

115

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This study describes the identification of Drosophila yellow-f and yellow-f2 as dopachrome-conversion enzymes responsible for catalysing the conversion of dopachrome into 5,6-dihydroxyindole in the melanization pathway. Drosophilayellow-y gene and yellow-b, -c, -f and -f2 genes were expressed in an insect cell/baculovirus expression system and their corresponding recombinant proteins were screened for dopachrome-conversion enzyme activity. Among the yellow and yellow-related genes, the yellow-f and yellow-f2 genes were identified as the genes coding for Drosophila dopachrome-conversion enzyme based on the high activity of their recombinant proteins in catalysing the production of 5,6-dihydroxyindole from dopachrome. Both yellow-f and yellow-f2 are capable of mediating a decarboxylative structural rearrangement of dopachrome, as well as an isomerization/tautomerization of dopamine chrome and dopa methyl ester chrome. Northern hybridization revealed the transcription of yellow-f in larvae and pupae, but a high abundance of mRNA was observed in later larval and early pupal stages. In contrast, yellow-f2 transcripts were present at all stages, but high abundance of its mRNA was observed in later-stage pupae and adults. These data indicate that yellow-f and yellow-f2 complement each other during Drosophila development and that the yellow-f is involved in larval and pupal melanization, and yellow-f2 plays a major role in melanization reactions in Drosophila during later pupal and adult development. Results from this study provide the groundwork towards a better understanding of the physiological roles of the Drosophilayellow gene family.

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“…In this family five species of proteins (apalbumin 1-5) with molecular masses ranging from 49-87 kDa have been identified [33]. Apalbumin 3 exists in five isoforms.…”

Section: Introductionmentioning

confidence: 99%

“…Its mRNA has been found expressed in the mushroom bodies of the adult honeybee brain [37] and in the hypopharingeal glands of both nurse bees and foragers [18,36,38]. Apalbumin 1 has been investigated by using cDNA cloning, immunoblotting, SDS-PAGE and 2-DE electrophoresis [15,18,33,35].…”

Section: Introductionmentioning

confidence: 99%

Towards royal jelly proteome

et al. 2005

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The recent availability of the honey-bee Apis mellifera genome and trascriptome of both the female castes, has stimulated new efforts in investigating the protein composition of royal jelly (RJ), its role in caste differentiation and its quality and typicality by a proteomic approach. This study is aimed both to separate and identify proteins of royal jelly and to detect some of them in honey-bee pollen-bread by using two-dimensional gel electrophoresis, mass spectrometry and by de novo sequencing. All the identified proteins belonged to the Apis mellifera genome. Apalbumin 1 was also confirmed to be present in honey-bee pollen-bread where the presence of apalbumin 2 was also found. In addition several fragments of apalbumin 1 and apalbumin 3 were also found in RJ. These could be the result of protease activity other than that of serine-protease. This study is a contribution to the description of royal jelly proteome.

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A family of major royal jelly proteins of the honeybee Apis mellifera L.

Cited by 284 publications

References 48 publications

Quality of royal jelly produced by Africanized honeybees fed a supplemented diet

Quality of royal jelly produced by Africanized honeybees fed a supplemented diet

Identification of Drosophila melanogaster yellow-f and yellow-f2 proteins as dopachrome-conversion enzymes

Towards royal jelly proteome

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