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Molecular cloning, characterization and expression of the energy homeostasis-associated gene in piglet 被引量:1
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作者 Sheng-ping WANG Yun-ling GAO +8 位作者 Gang LIU Dun DENG Rong-jun CHEN Yu-zhe ZHANG Li-li LI Qing-qi WEN Yong-qing HOU ze-meng feng Zhao-hui GUO 《Journal of Zhejiang University-Science B(Biomedicine & Biotechnology)》 SCIE CAS CSCD 2015年第6期524-532,共9页
The energy homeostasis-associated(Enho) gene encodes a secreted protein, adropin, which regulates the expression of hepatic lipogenic genes and adipose tissue peroxisome proliferator-activated receptor γ, a major r... The energy homeostasis-associated(Enho) gene encodes a secreted protein, adropin, which regulates the expression of hepatic lipogenic genes and adipose tissue peroxisome proliferator-activated receptor γ, a major regulator of lipogenesis. In the present study, the porcine(Sus scrofa) homologue of the Enho gene, which was named p Enho, was amplified by reverse transcriptase polymerase chain reaction(RT-PCR) using oligonucleotide primers derived from in silico sequences. The gene sequence was submitted into the Gen Bank of NCBI, and the access number is GQ414763. The p Enho encodes a protein of 76 amino acids which shows 75% similarity to Homo sapiens adropin. The expression profile of p Enho in tissues(liver, muscle, anterior jejunum, posterior jejunum, and ileum) was determined by quantitative real-time RT-PCR. p Enho was localized on porcine chromosome 10 and no introns were found. In conclusion, p Enho was cloned and analysed with the aim of increasing knowledge about glucose and lipid metabolism in piglets and helping to promote the health and growth of piglets through adropin regulation. 展开更多
关键词 Adropin Energy homeostasis-associated(Enho) gene Gene coloning PIGLETS RT-PCR
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An Enzyme-Free Amperometric Sensor Based on Self-Assembling Ferrocene-Conjugated Oligopeptide for Specific Determination of L-Arginine 被引量:1
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作者 Kai-Jie Zhu Li Zhou +8 位作者 Ling Wu Sai-Fei feng Hui-Ying Hu Jing-Lin He Yu-Min He ze-meng feng Yu-Long Yin Donghong Yu Zhong Cao 《Chinese Journal of Chemistry》 SCIE CAS CSCD 2021年第10期2755-2762,共8页
Main observation and conclusion An enzyme-free amperometric sensor based on a heptadecapeptide possessing an electroactive ferrocene(Fc)linker as ferrocene-Gly-Gly-Gly-Gly-Phe-Gly-His-Ile-His-Glu-Gly-Tyr-Gly-Gly-Gly-G... Main observation and conclusion An enzyme-free amperometric sensor based on a heptadecapeptide possessing an electroactive ferrocene(Fc)linker as ferrocene-Gly-Gly-Gly-Gly-Phe-Gly-His-Ile-His-Glu-Gly-Tyr-Gly-Gly-Gly-Gly-Lys-(CH_(2))_(4)-dithiocyclopentane self-assembled on gold substrate was designed and fabricated for specific determination of L-arginine(L-Arg).The detection mechanism is based on conformational change of surface-immobilized peptide induced by the target L-Arg,which was confirmed via SEM,TEM,AFM,XPS,and SPR studies.The binding affinity and the recognition feasibility of immobilized specific and non-specific peptides were also assessed using electrochemical impedance spectroscopy(EIS),cyclic voltammetry(CV),and differential pulse voltammetry(DPV).The proposed method can serve as“signal-on”sensor for detection of L-Arg down to 31 pmol/L with broad linear range(0.0001 to 10μmol/L).Furthermore,the Fc-conjugated specific peptide sensor was successfully applied to the determination of L-Arg in pig serums with a recovery rate of 97.5%—106.9%,and its test results are in good agreement with that of chromatographic instrument,evidencing that the oligopeptide-based sensor can be served as a simple and enzyme-free biosensing platform towards L-Arg for future application. 展开更多
关键词 L-ARGININE Peptides Surface Analysis Enzyme-Free Amperometric Sensor
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