Studies on Protein in Royal Jelly 2. Fractionation of Water-Soluble Protein by Deae-Cellulose Chromatography, Gel Filtration and Disc Electrophoresis

Tomoda, Goro; Matsuyama, Jun; Matsuka, Mitsuo

doi:10.1080/00218839.1977.11099873

Cited by 14 publications

(5 citation statements)

References 6 publications

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“…They fluctuated between 56-86% of TP. Observed fluctuations are in good agreement with previous measurements of WSPs (46-89%, Tomoda et al 1977;Takenaka & Echigo 1983). Defensin1 gene expression was studied in nurses having developed LJproducing cephalic glands (Lensky & Rakover 1983;Knecht & Kaatz 1990;Klaudiny et al 2005) using for normalization transcripts of genes encoding constitutive LJ proteins, MRJP3 and MRJP4 (Klaudiny et al 1994a, b;Schmitzová et al 1998;Albert et al 1999).…”

Section: Discussionsupporting

confidence: 70%

“…Development of a procedure for the quantification of defensin1 in LJs Since RJ contains water soluble as well as insoluble proteins (Tomoda et al 1977;Takenaka & Echigo 1983) it cannot be excluded that certain portion of defensin1 fractionates with insoluble protein fraction of LJ. Therefore, for the determination of defensin1 amounts in jellies, immunoblotting was chosen by which denaturing conditions used for preparation of samples solubilize most molecular complexes and protein aggregates.…”

Section: Resultsmentioning

confidence: 99%

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Expression of larval jelly antimicrobial peptide defensin1 in Apis mellifera colonies

et al. 2012

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Honeybee brood food, larval jelly (LJ) contains antimicrobial peptide defensin1 that is able to inhibit in vitro growth of the pathogen causing American foulbrood (AFB). This fact suggests that LJ defensin1 could participate in defense of colonies against AFB. We assume that the potential defense function of defensin1 in vivo might depend on its amount in LJs. Therefore, we investigated the expression of defensin1 in colonies. The expression was examined on protein and mRNA levels in colonies of several Apis mellifera carnica lines collected in 3 apiaries (1 infected with AFB) with the aim to identify factors influencing the expression. Levels of defensin1 were determined in royal and worker jellies by a developed immunoblot procedure employing antibodies generated against the recombinant peptide. Defensin1 mRNA levels in nurse heads were explored by dot blot hybridization using transcript of two MRJP genes for normalization. Analyzed LJs contained various amounts of defensin1 (0.159-0.524 µg/mg jelly). Higher variations in defensin1 levels were observed among LJ samples collected from different colonies than among those collected within single colony. Colonies producing LJs with elevated defensin1 levels occurred among various honeybee lines. Levels of defensin1 mRNA varied in heads of nurses and the variations correlated with defensin1 peptide levels in LJs only in some colonies. Obtained data demonstrate that defensin1 is constitutively expressed into LJs in colonies and indicate that its levels in jellies are determined by genetic factors regulating transcription and/or translation/posttranslation processes in nurses. AFB infection, larval age and type of LJ do not seem to affect the levels of the peptide in LJs. Findings made in this work suggest that it should be possible to breed novel honeybee lines expressing higher amounts of defensin1 into LJs.

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Section: Discussionsupporting

confidence: 70%

Section: Resultsmentioning

confidence: 99%

Expression of larval jelly antimicrobial peptide defensin1 in Apis mellifera colonies

et al. 2012

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“…Varying data on content of WSPs (including MRJPs) in total RJ protein (46-89%), have been reported [16][17][18]. Electrophoresis ( fig.…”

Section: The Electrophoretic and Quantitative Analyses Of Mrjps In Rjmentioning

confidence: 99%

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

Schmitzová¹,

Klaudiny²,

Albert³

et al. 1998

CMLS, Cell. Mol. Life Sci.

277

337

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The characterization of major proteins of honeybee larval jelly (49-87 kDa) was performed by the sequencing of new complementary DNAs (cDNAs) obtained from a honeybee head cDNA library, by the determination of N-terminal sequences of the proteins, and by analyses of the newly obtained and known sequence data concerning the proteins. It was found that royal jelly (RJ) and worker jelly (WJ) contain identical major proteins and that all the proteins belong to one protein family designated MRJP (from Major Royal Jelly Proteins). The family consists of five main members (MRJP1, MRJP2, MRJP3, MRJP4, MRJP5). The proteins MRJP3 and MRJP5 are polymorphic. MRJPs account for 82 to 90% of total larval jelly protein, and they contain a relatively high amount of essential amino acids. These findings support the idea that MRJPs play an important role in honeybee nutrition.

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“…slightly pungent in odour and taste and made up o'i proteins. tVee amino acids, fatty acids, sugars, vitatnins and some minerals [1][2][3][4][5][6]. During the early stages of development, royal jelly is the only food of female bee larvae but only (he queen bee continues to receive this did while other larvae develop itito sexually immature worker bees.…”

Section: Introductionmentioning

confidence: 99%