• International Journal of Industrial Entomology and Biomaterials
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• 제18권2호
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• pp.139-142
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• 2009

The histological and transmission electron microscopic studies revealed the synthesis activity predominantly in the hypopharyngeal glands of the nurse bees. The biochemical analysis of both, the hypopharyngeal gland extract and royal jelly elucidated unequivocally the proteins and lipids as the major constituents. Further the SDS-PAGE of hypopharyngeal gland extract showed about 17 protein bands, perhaps 14.10, 20.00, 29.00 and 43.00 kDa predominantly while that of royal jelly revealed only two protein bands of 29.00 and 43.00 kDa molecular weight suggesting them as the major royal jelly proteins (MRJP). The lipid profile of royal jelly consists of triglycerides, cholesterol, HDL, LDL and VLDL.

• 한국양봉학회지
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• 제32권3호
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• pp.155-162
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• 2017

로얄제리 생산성 우수계통 선발을 위해 국내 육성서양종꿀벌 원종 계통인 A와 C에 대한 로얄제리 생산성 및 접수율 평가를 수행하였다. 그 결과 꿀벌 계통C의 로얄제리 생산량은 $33.7{\pm}7.41g$로A 계통에 비해 높은 것으로 드러났으며, 접수율 또한 $87.8{\pm}7.5%$로 A 계통에 비해 높은 것으로 확인되었다. 이들 계통으로부터 생산된 로얄제리 trans-10-hydroxy-2-decenoic acid (10-HDA) 함량을 분석한 결과 꿀벌 계통 C는 4.28%(${\pm}0.3$)으로, A 계통에 비해 높은 것으로 나타났다. 일령에 따른 major royal jelly proteins(MRJPs) 전사체 발현량을 비교한 결과 10일령의 일벌의 경우 C 계통이 A 계통에 비해 MRJP 발현량이 큰 폭으로 증가했음을 확인 할 수 있었으며, 15일령의 일벌의 MRJP 발현량 또한 C계통이 A 계통에 비해 높은 것을 확인할 수 있었다. 이러한 결과를 통해 본 연구에서는 국내 육성 서양종꿀벌 기본종 계통 중 로얄제리 생산성이 가장 우수한 계통은 C 계통인 것으로 평가 되었으며, 향후 로얄제리 생산성 우수 계통 선발을 위한 기초 자료로 제공 될 수 있을 것이라 기대하고 있다.

• BMB Reports
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• 제36권6호
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• pp.572-579
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• 2003

An expressed sequence tag (EST) library was established from the hypopharyngeal glands of Apis cerana. Sixty-six recombinant clones, possessing inserts >500 bp, were randomly selected and unidirectional sequenced. Forty-two of these (63.6%) were identified as homologues of Major Royal Jelly Proteins families 1, 2, 3, and 4 of A. mellifera (AmMRJP) for which MRJP1 was the most abundant family. The open-reading frame of the MRJP1 homologue (AcMRJP1) was 1299 nucleotides that encoded 433 deduced amino acids with three predicted N-linked glycosylation sites. The AcMRJP1 sequence showed 93% and 90% homologies with nucleotide and deduced amino acid sequences of AmMRJP1, respectively. Two complete transcripts of apisimin, and one and two partial transcripts of $\alpha$-glucosidase and glucose oxidase, were also isolated. In addition, the royal jelly proteins of A. cerana were purified and characterized using Q-Sepharose and Sephadex G-200 column chromatography. The native forms of protein peaks A1, A2, B1, and C1 were 115, 55, 50, and 300 kDa, respectively. SDS-PAGE analysis indicated that A1 and C1 were dimeric and oligomeric forms of the 80 kDa and 50 kDa subunits, respectively. The ratio of the total protein quantities of A1 : A2 : B1 : C1 were 2.52 : 4.72 : 1 : 12.21. Further characterization of each protein, using N-terminal and internal peptide sequencing, revealed that the respective proteins were homologues of MRJP3, MRJP2, MRJP1, and MRJP1 of A. mellifera.

• BMB Reports
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• 제38권1호
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• pp.49-57
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• 2005

Major Royal Jelly Protein cDNAs of Apis cerana (AcMRJP) were cloned and characterized. The open reading frames (ORFs) of the AcMRJP1 and AcMRJP2 genes were 1302 and 1392 nucleotides, encoding 433 and 463 amino acid residues, respectively. The sequence divergences between AcMRJP1 and AcMRJP2 and their corresponding protein families in A. mellifera were 0.0618 and 0.0934 at the nucleotide level and 0.0912 and 0.1438 at the protein level, respectively. Phylogenetic analysis supports the orthologous similarity between these proteins. The deduced amino acids indicated high essential amino acid contents of AcMRJP1 and AcMRJP2 (47.5 and 44.8%, respectively). The genomic organization of both AcMRJP1 and AcMRJP2 was determined. Both the AcMRJP1 (3663 bp) and AcMRJP2 (3963 bp) genes contained six exons and five introns, where all boundaries conformed to the GT/AG rule. AcMRJP1 and AcMRJP2 cDNAs were cloned into pET17b, and both the recombinant (r) AcMRJP1 (47.9 kDa) and rAcMRJP2 (51.7 kDa) were expressed in the insoluble form. Western blot analysis and N-terminal sequencing of the solubilized proteins revealed successful expression of rAcMRJP1 and rAcMRJP2 in vitro. The yields of the purified rAcMRJP1 and rAcMRJP2 were approximately 20 and 8mg protein per liter of the flask culture, respectively.