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Cloning and mRNA Expression of an Actin cDNA from the Mulberry Longicorn Beetle, Apriona germari
Gui, Zhongzheng,Lee, Kwang Sik,Wei, Yadong,Yoon, Hyung Joo,Kim, Iksoo,Guo, Xijie,Sohn, Hung Dae,Jin, Byung Rae Korean Society of Sericultural Science 2004 International Journal of Industrial Entomology Vol.9 No.2
Actin is a ubiquitous and highly conserved protein found in eukaryotic organisms. In this study, we describe the cDNA cloning and mRNA expression of an actin gene from the mulberry longicorn beetle, Apriona germari. The A. germari actin cDNA is 1524 bp containing a complete 1128 bp open reading frame that encodes a polypeptide of 376 amino acid residues with a predicted molecular weight of about 41.5 kDa. The deduced amino acid sequence of the A.germari actin cDNA showed 99% protein sequence identity to Homalodisca coagulata actin, differing at only two amino acid positions, and 92-98% protein sequence identity to known insect species actins. The predicted three-dimensional structure of A. germari actin revealed the four residue hydrophobic pulg loop characteristic of the actin family. Northern blot analysis showed that A. germari actin is highly expressed in epidermis and muscle, and less strongly in midgut, but not in the fat body of A. germari larva.
Molecular Cloning of a LIM Protein cDNA from the Mulberry Longicorn Beetle, Apriona germari
Gui, Zhongzheng,Wei, Yadong,Yoon, Hyung Joo,Kim, Iksoo,Guo, Xijie,Jin, Byung Rae,Sohn, Hung Dae Korean Society of Sericultural Science 2004 International Journal of Industrial Entomology Vol.9 No.1
Here we report the molecular cloning of a LIM protein cDNA of the CRP (cysteine-rich protein) family from the mulberry longicorn beetle, Apriona, geramri. The A. germari LIM protein cDNA contains an open reading frame of 276 bp encoding 92 amino acid residues with a calculated molecular weight of approximately 10 kDa. The A. germari LIM protein contains the cysteine-rich consensus sequence of LIM domain and the glycine-rich consensus sequence observed in cysteine-rich protein family 1 (CRP1). The potential nuclear targeting signal is retained. The deduced amino acid sequence of the A. germari LIM protein cDNA showed 81 % identity to both Bombyx mori muscle LIM protein (Mlp) and Drosophila melanogaster Mlp60A and 77% to Epiblema scudderiana Mlp. Northern blot analysis showed that A. germari LIM protein is highly expressed in epidermis and muscle, and less strongly in midgut, but not in the fat body.
The Physical Methods for Induction of Anti-Bacterial Substances in the Silkworm Larva, Bombyx mori
Gui, Zhongzheng,Dai, Jianyi,Zhuang, Dahuan Korean Society of Sericultural Science 2003 International Journal of Industrial Entomology Vol.7 No.2
To understand the physical method for induction of anti-bacterial substances from the silkworm larvae, Bombyx mori, three physical methods, i.e., infrared radiation, ultraviolet radiation and ultrasonic wave, have been used in this study. The results have shown that ultrasonic wave can induce anti-bacterial sub-stances effectively than radiations in the B. mori larva. The induction of anti-bacterial substances was different from silkworm race to race. Summer-autumn silkworm race (Qiufeng${\times}$Baiyu) was easy to induce antibacterial substances. It is suggested that the ultrasonic wave is a simple and easy method for induction.
Molecular Cloning of a Profilin cDNA from Bombyx mori
Wei, Yadong,Gui, Zhongzheng,Choi, Young Soo,Guo, Xijie,Zhang, Guozheng,Sohn, Hung Dae,Jin, Byung Rae Korean Society of Sericultural Science 2004 International Journal of Industrial Entomology Vol.9 No.1
The actin-binding protein profilin cDNA was firstly isolated from the lepidopteran insect, silkworm Bombyx mori. The B. mori profilin cDNA contains an open reading frame of 378 bp encoding 126 amino acid residues and possesses three cysteine residues. The deduced amino acid sequence of the B. mori profilin cDNA showed 80% identity to Apis mellifera profilin and 72% to Drosophila melanogaster profilin. Northern blot analysis showed that B. mori profilin is highly expressed in epidermis and less strongly in silk gland. In addition, Northern blot analysis revealed the presence of B. mori profilin transcripts in all tissues examined, suggesting that B. mori profilin gene is expressed in most, if not all, body tissues.
PCR-Based Detection of Densovirus Infection in Silkworm (Bombyx mori L.)
Hou Chengxiang,Li Muwang,Gui Zhongzheng,Xu Anying,Guo Xijie Korean Society of Sericultural Science 2005 International Journal of Industrial Entomology Vol.11 No.2
Two pairs of DNA primers were designed for the detection of the Zhenjiang (China) strain of Bombyx mori densonucleosis virus (BmDNV-Z). These primers were designed from the nucleotide sequence of major structural protein gene (putative VD1-ORF2). PCR amplification was attempted from different issues (including silk gland, blood, skin and midgut) and feces of the silkworm which infected wit BmDNV-Z were amplified by PCR. Both of the primers gave expected size of in the DNA bands from midgut and feces, but not in the DNA of silk gland, blood and skin. The two bands were sequenced, and their sequence were same as the sequence designed for. BmDNV-Z could be successfully detected in single silkworm after it was infected for 12 hrs, and could not be detected before 9 hrs after infected.
Ionic liquid extraction of silkworm pupa protein and its biological characteristics
Zeng Qing-Lei,Zhang Ning,Zhang Yue-Yue,Xin Xiang-Dong,Attaribo Thomas,Shao Ying,Tang Liu-Mei,Zhang Ran,이광식,진병래,Gui Zhongzheng 한국응용곤충학회 2021 Journal of Asia-Pacific Entomology Vol.24 No.1
Silkworm (Bombyx mori) pupa protein (SPP) is a high-quality source of animal protein with substantial nutri tional benefits and health value. To develop an efficient extraction method for SPP that is environmentally friendly, we selected choline hydroxide ionic liquid (CH-IL) as the extraction solvent and performed orthogonal experiments to optimize the extraction conditions. We demonstrated that 3% CH-IL, a solid-to-liquid ratio (g/mL) of 1:30, an extraction temperature of 40 ◦ C, and an extraction time of 1 h facilitated the most efficient extraction. Compared to the conventional alkali solubilization–acid precipitation method, the CH-IL extraction increased protein content by 12.14%. Protein structure analysis showed that the β-sheet content increased by 10.98% and that of disulfide bonds reduced by 16.4%. The processing properties of the CH-IL extracted protein showed that the solubility, emulsification, and foaming capacity were enhanced by 82.87%, 15.44%, and 18.97%, respec tively. The physical properties of SPP remarkably improved relative to the increased stretching of the poly peptide chains. The findings of this study provide technical knowledge that will enhance the processing performance of pupal proteins.