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- 저자 : Xiao‑an Cao (검색결과 4 건)
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Xiao‑xia Ma,Yi‑ning Wang,Xiao‑an Cao,Xue‑rui Li,Yong‑sheng Liu,Jian‑hua Zhou,Xue‑peng Cai 한국유전학회 2018 Genes & Genomics Vol.40 No.9
The nucleocapsid (N) protein of peste des petits ruminants virus (PPRV) with a conserved amino acid usage pattern plays an important role in viral replication. The primary objective of this study was to estimate roles of synonymous codon usages of PPRV N gene and tRNA abundances of host in the formation of secondary structure of N protein. The potential effects of synonymous codon usages of N gene and tRNA abundances of host on shaping different folding units (α-helix, β-strand and the coil) in N protein were estimated, based on the information about the modeling secondary structure of PPRV N protein. The synonymous codon usage bias was found in different folding units in PPRV N protein. To better understand the role of translation speed caused by variant tRNA abundances in shaping the specific folding unit in N protein, we modeled the changing trends of tRNA abundance at the transition boundaries from one folding unit to another folding unit (β-strand → coil, coil → β-strand, α-helix → coil, coil → α-helix). The obvious fluctuations of tRNA abundance were identified at the two transition boundaries (β-strand → coil and coil → β-strand) in PPRV N protein. Our findings suggested that viral synonymous codon usage bias and cellular tRNA abundance variation might have potential effects on the formation of secondary structure of PPRV N protein.
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Ann, Xiao-Hua,Lun, Yong-Zhi,Zhang, Wei,Liu, Ben,Li, Xing-Yun,Zhong, Min-Tao,Wang, Xiao-Li,Cao, Jing,Ning, An-Hong,Huang, Min Asian Pacific Journal of Cancer Prevention 2014 Asian Pacific journal of cancer prevention Vol.15 No.12
In this study, an anti-oxidant and anti-tumor protein Latcripin-3 of Lentinula edodes C91-3 was expressed in Escherichia coli. for the first time. According to the cDNA library, the full-length gene of Latcripin-3 was cloned by the methods of 3'-full rapid amplification of cDNA Ends (RACE) and 5'-full RACE. The structural domain gene of Latcripin-3 was inserted into the pET32 a(+). The functional protein of Latcripin-3 was expressed in Rosetta-gami (DE3) E. coli, evaluated by Western blotting and mass spectrometry. DPPH testing showed that the protein Latcripin-3 can scavenge free radicals remarkably well. The activity of functional protein Latcripin-3 on A549 cells was studied with flow cytometry and the MTT method. The MTT assay results showed that there was a decreases in cell viability in a dose-dependent and time-dependent manner in protein Latcripin-3 treated groups. Flow cytometry demonstrated that Latcripin-3 can induce apoptosis and block S phase dramatically in human A549 lung cancer cells as compared to the control group. At the same time, the cell ultrastructure observed by transmission electron microscopy supported the results of flow cytometry. This research offers new insights and advantages for identifying anti-oxidant and anti-tumor proteins.
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Anomalous magnetization jumps in granular Pb superconducting films
Zhang An-Lei,Jiang Wan-Yan,Chen Xing-Hong,Zhang Xiao-Ke,Lu Wen-Lai,Chen Fei,Feng Zhen-Jie,Cao Shi-Xun,Zhang Jin-Cang,Ge Jun-Yi 한국물리학회 2022 Current Applied Physics Vol.35 No.-
In granular superconductors, the grain boundaries are closely related to the vortex dynamics and the macroscopic superconducting properties. In our research, Pb films with different grain sizes were prepared by tuning the substrate temperature. With the grain size decreasing, Pb films are prone to feature the anomalous magnetization jumps in the M − T curves, while in the M − H curves flux avalanche happens. Both phenomena appear in the same region of the H − T phase diagram and thus are considered to have the same origin. The further theoretical analysis shows that with grain size decreasing the pinning mechanism evolves from a mixed δTc and δl pinning to the δl pinning mechanism. The results shed light on the study of pinning mechanism for granular superconductors and is beneficial to the potential application of manipulating vortex pinning by regulation of intrinsic defects.
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Secretory Expression and Purification of the Recombinant Duck Interleukin-2 in Pichia pastoris
( Cui Hong Du ),( Long Han ),( An Feng Xiao ),( Min Jie Cao ) 한국미생물 · 생명공학회 2011 Journal of microbiology and biotechnology Vol.21 No.12
Interleukin-2 (IL-2) is a vital cytokine secreted by activated T lymphocytes, and plays an important role in the regulation of cellular functions and immunity of animals. In this study, the recombinant duck IL-2 (rduIL-2) was secretory expressed in Pichia pastoris (P. pastoris). The recombinant P. pastoris strain was cultured in shake flasks and then scaled up in a 5.0-l bioreactor. The result showed that the maximal fresh-cell-weight of 594.1 g/l and the maximal OD600 of 408 were achieved in the bioreactor. The rduIL-2 was purified by two steps of purification procedures, and approximately 311 mg of rduIL-2/L fermentation supernatant was obtained. SDS-PAGE showed that the purified rduIL-2 constituted a homogeneous band of ~16 kDa or ~14 kDa corresponding to the glycosylated or non-glycosylated duIL-2 protein in size, respectively. The bioactivity of rduIL-2 was determined by lymphocyte proliferation assay. The result indicated that the rduIL-2 greatly promoted the proliferation of ConA-stimulated lymphocytes in vitro. The P. pastoris expression system described here could provide promising, inexpensive, and large-scale production of the rduIL-2, which lays the foundation for development of novel immunoadjuvants to enhance both the immunity of ducks against various infectious pathogens and vaccine efficacy.
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