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Acta Oceanologica Sinica 2005年第2期24卷 113-119页

作者： QIULihua SONGLinsheng WULongtao XUWei JIANGShigui InstituteofOceanology ChineseAcademyofSciencesQingdao266071China／／SouthChinaSeaFisheriesResearchInstituteChineseAcademyofFisherySciencesGuangzhou510300China InstituteofOceanology ChineseAcademyofSciencesQingdao266071China InstituteofOceanology ChineseAcademyofSciencesQingdao266071China／／GraduateSchoolChineseAcademyofSciencesBeijingI00039China SouthChinaSeaFisheriesResearchInstitute ChineseAcademyofFisherySciencesGuangzhou510300China

A homologue of the lower vertebrates translationally controlled tumor protein (TCTP) was cloned from the marine fish Japanese sea perch (Lateolabrax japonicus) by the technology of homology cloning. The full-length cdna sequence of the sea perch TCTP gene contained a 5' untranslated region (UTR) of 47 bp, a 3' UTR of 433 bp, and a putative open reading frame (ORF) of 510 bp encoding a polypeptide of 170 amino acids. The deduced amino acid sequence of the sea perch TCTP gene showed a high similarity to that of zebrafish, rohu, rabbit, chicken and human. Sequence analysis revealed there were a signature sequence of TCTP family, an N-glycosylation site, and five Casein kinase phosphorylation sites in the sea perch TCTP. The temporal expression of TCTP genes in healthy and lipopolysaccharide (LPS) challenged fishes was measured by semi-quantitative reverse transcription-PCR (RT-PCR). The results indicated that LPS could up-regulate the expression of sea perch TCTP in the examined tissues, including head-kidney, spleen and liver.

关键词： translationally controlled tumor protein Lateolabrax japonicus cdna cloning mRNA expression

cdna cloning of a novel lectin that induce cell apoptosis from Artocarpus hypargyreus

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Chinese Journal of Natural Medicines 2021年第2期19卷 81-89页

作者： LUO Yu ZENG Lin-Jie LIU Xiao-Qin LI Lu ZENG Qi-Yan Department of Biochemistry and Molecular Biology Guangxi Medical UniversityNanning 530021China Department of Orthopaedics Chinese and Western Orthopaedics Hospital of GuigangGuigang 537100China

We isolated a novel lectin(AHL)from Artocarpus hypargyreus Hance and showed its immunomodulatory *** this study,the amino acid sequence of AHL was determined by cdna *** cdna(875bp)contains a 456-bp open reading frame(ORF),which encodes a protein with 151 amino *** is a new member of jacalin-related lectin family(JRLs),which share high sequence similarities to KM+and Morniga M,and contain the conserved carbohydrate binding *** antitumor activity of AHL was also explored using Jurkat T cell *** exhibits a strong binding affinity to cell membrane,which can be effectively inhibited by methyl-α-*** inhibits cell proliferation in a time-and dose-dependent manner through apoptosis,evidenced by morphological changes,phosphatidylserine externalization,poly ADP-ribose polymerase(PARP)cleavage,Bad and Bax up-regulation,and caspase-3 *** further showed that the activation of ERK and p38 signaling pathways is involved for the pro-apoptotic effect of AHL.

关键词： Lectin cdna cloning Apoptosis Antitumor drug Artocarpus hypargyreus

Two Divergent Members of 4-Coumarate： Coenzyme A Ligase from Salvia miltiorrhiza Bunge： cdna cloning and Functional Study

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Journal of Integrative Plant Biology 2006年第11期48卷 1355-1364页

作者： Shu-Juan Zhao Zhi-Bi Hu DI Liu Frederick C. C. Leungt Institute of Traditional Chinese Materia Medica Shanghai University of Traditional Chinese Medicine Shanghai 201203 China Department of Zoology University of Hong Kong Hong Kong SAR China

4-Coumarate ： coenzyme A Ilgase （4CL） Is one of the key enzymes In phenylpropanoid metabolism leading to series of phenollcs, Including water-soluble phenolic acids, which are important compounds determining the medicinal quality of Danshen （Salvia miltiorrhiza Bunge）, a traditional Chinese medicinal herb. To Investigate the function of 4CL in the biosynthesis of water-soluble phenolic acid in Danshen, we have cloned two cdnas （Sm4CL1 and Sm4CL2） encoding divergent 4CL members by applying nested reverse transcrlptlon-polymerase chain reaction （RT-PCR） with degenerate primers followed by 5′/3′rapid amplification of cdna ends （RACE）（Note, these sequence data have been submitted to the GenBank database under accession numbers AY237163 and AY237164）. Either of the coding regions was inserted into a pRSET vector and a kinetic assay was performed with purified recombinant proteins. The substrate utilization profile of Sm4CL1 was distinct from that of Sm4CL2. The Km values of Sm4CL1 and Sm4CL2 to 4-coumarlc acid were （72.20±4.10） and （6.50±1.45） μmol/L, respectively. These results, In conjunction with Northern blotting and other information, imply that Sm4CL2 may play an Important role in the biosynthesis of watersoluble phenolic compounds, whereas Sm4CL1 may play a minor role in the pathway. Southern blotting analysis suggested that both Sm4CL1 and Sm4CL2 genes are present as a single copy and are located at different sites In the genome.

关键词： cdna cloning 4-coumarate : coenzyme A ligase (4CL) Danshen (Salvia miltiorrhiza) enzymatic kinetic assays water-soluble phenolic acids.

cdna cloning of Two Novel T-superfamily Conotoxins from Conus leopardus

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Acta Biochimica et Biophysica Sinica 2006年第4期38卷 287-291页

作者： Wei-Hua CHEN~(1,2#) Yu-Hong HAN~(2,3#) Qi WANG~(2,3#) Xiao-Wei MIAO~(2,4) Ling OU~1 Xiao-Xia SHAO~2* 1 Bioengineering Institute,East China University of Science and Technology,Shanghai 200237,China 2 Institute of Protein Research,Tongji University,Shanghai 200092,China 3 Institute of Biochemistry and Cell Biology,Shanghai Institute of Biochemical Sciences,Chinese Academy of Sciences,Shanghai 200031,China 4 Department of Biological Engineering,School of Life Science,Shanghai University,Shanghai 200436,China Bioengineering Institute East China University of Science and Technology Shanghai 200237 China

The full-length cdnas of two novel T-superfamily conotoxins,Lp5.1 and Lp5.2,were clonedfrom a vermivorous cone snail Conus leopardus using 3'/5'-rapid amplification of cdna *** cdna ofLp5.1 encodes a precursor of 65 residues,including a 22-residue signal peptide,a 28-residue propeptide anda 15-residue mature ***5.1 is processed at the common signal site -X-Arg- immediately before themature peptide *** the case of Lp5.2,the precursor includes a 25-residue signal peptide anda 43-residue sequence comprising the propeptide and mature peptide,which is probably cleaved to yield a29-residue propeptide and a 14-residue mature *** these two conotoxins share a similar signalsequence and a conserved disulfide pattern with the known T-superfamily,the pro-region and mature peptidesare of low identity,especially Lp5.2 with an identity as low as 10.7% compared with the reference *** elucidated cdnas of these two toxins will facilitate a better understanding of the species distribution,the sequence diversity of T-superfamily conotoxins,the special gene structure and the evolution of thesepeptides.

关键词： Conus leopardus T-superfamily conotoxin cdna cloning

cdna cloning, Bioinformatic and Tissue-specific Expression Analysis of Porcine JARID1C Gene

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Journal of Genetics and Genomics 2007年第12期34卷 1088-1096页

作者：伊璐郝振华杨彤彤王邵兵邢宝松徐银学南京农业大学动物科技学院南京210095

Jumonji, AT-rich interactive domain 1C （JARID1C） protein belongs to the highly conserved ARID protein family, which is involved in chromatin remodeling and transcriptional regulation during cell growth, differentiation, and development. In humans, this gene plays a vital role in normal brain development and function. Using an in silico approach in combination with 5＇ rapid amplification of cdna ends （5＇ RACE）, the full-length cdna of JARIDIC （GenBank accession No. EF139241） from porcine ovary, which contains 5,908 bp nucleotides, with an open reading frame （ORF） of 4,548 bp, has been cloned. The putative porcine JARID 1C protein, which is located in the nucleus, encodes 1,516 amino acids with a molecular weight of 170 kDa and a pI of 5.44. Bioinformatic prediction indicates that the protein contains several conserved domains： a JmjN domain, an ARID domain, a JmjC domain, a C5HC2 zinc finger domain, and a PHD zinc finger domain. Similarity comparisons for nucleic and amino acid sequences reveal that the porcine JARID1C protein shares a high identity with its dog, mouse, rat, and human counterparts. The phylogenetic tree of the JARID1 subfamily proteins has been constructed to reveal the evolutionary relationship of various species. Real-time PCR analysis shows that the JARIDIC gene is expressed in various tissues, but at different levels. The expression levels of this gene are higher in the brain and gonad than in other tissues, suggesting that the JARID1C protein plays a role in porcine brain and gonad functions.

关键词： pig JARID1C gene cdna cloning bioinformatic analysis gene expression

UGPase of Astragalus membranaceus : cdna cloning, Analyzing and Expressing in Escherichia coli

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Acta Botanica Sinica 2002年第6期44卷 689-693页

作者：吴晓俊杜旻翁颖琦刘涤胡之璧上海中医药研究院中药研究所上海200032

On the basis of sequences of UGPase from plants, a cdna encoding the enzyme was isolated from the hairy root of Astragalus membranaceus (Fisch.) Bunge. The cdna consisted of 1 831 bp and encoded a polypeptide of 471 amino acid residues with a calculated molecular weight of 51.5 kD and a deduced isoelectric point of 6.01. Then the open read frame of the cdna was ligated into pET28(a) + vector and expressed in E. coli BL21. SDS_PAGE showed that the expressed protein was ca. 40% in the total bacterial protein. Enzyme activity assay demonstrated that the UGPase activity in the transformed bacteria was 0.50-3.27 times higher than that of the control. Northern blotting revealed that ugp was expressed in the leaf, stem, root and hairy root of A. membranaceus , with a higher level in root and hairy root.

关键词： prokaryotic expression cdna cloning UGPase hairy root Astragalus membranaceus

Snake Serum Albumin as an Inhibitor of Venom Zinc Proteases:Purification,Characterization,and cdna cloning of Trimeresurus flavoviridis Serum Albumin

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Snake Serum Albumin as an Inhibitor of Venom Zinc Proteases:...

Purification,Characterization and cdna cloning of a Myofibril-bound Serine Proteinase from the Skeletal Muscle of Crucian Carp(Carassius auratus)

“基因、进化与生理功能多样性”海内外学术研讨会暨中国生理学会第七届比较生理学学术会议

作者： Xin-Rong Xing,Zhi-Kui Cheng,Wen-Dong Liu,Yong-De Hong,Hui-Jian Wu~* Department of Bioscience and Biotechnology,Dalian University of Technology,Dalian 116024

The protein inhibitor of metalloproteases in the venom of Habu snake Trimeresurus flavovirids was purified from the serum. This protein inhibited both proteolytic and fibrinolytic activies of zinc *** molecular weight was calculated to be approximately 67 kDa and 62 kDa with and without carbohydrates,*** ration of amino acid composition of the inhibitor showed a certain similarity to metalloprotease inhibitor designated HSF isolated from the serum of Habu snake Trimeresurus *** determination of the amino acid sequences for several peptide fragments,cdna cloning was performed to determine a full sequence of the *** inhibitor precursor was found to consist of the 584 amino acid residues,in which the inhibitor is with 558 residues and the signal peptide with 26 *** protein was judged to be a member of serum albumin, and the elucidated sequence was found to be very much similar to serum albumin of Naja naja *** inhibitor,namely,albumin, completely inhibited the lysis of fibrin, while other ordinary albumins from various sources exhibited no *** analysis suggested that the serum albumin of this particular toxic snake has evolved or co-evolved for detoxification.

关键词： Inhibitor Metalloprotease Purification cdna cloning Albumin

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Purification,Characterization and cDNA Cloning of a Myofibri...

Serum Inhibitor for the Trimeresurus Flavoviridis Venom Phospholipase A2:Purification,Characterization and cdna cloning

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作者： Chuan Guo~a Min-Jie Cao~(a*) Guang-Ming Liu~a Xiong-Shui Lin~a Kenji Hara~b Wen-Jin Su~a (~a College of Biological Engineering,The Key Laboratory of Science and Technology for Aquaculture and Food Safety,Jimei University,Xiamen,China,361021 ~bFaculty of Fisheries,Nagasaki University,Nagasaki,Japan,852-8521)

A myofibril-bound serine proteinase(MBSP)was highly purified from the skeletal muscle of crucian carp(carasius auratus)by acidic treatment of myofibril solution and chromatographies on Q-Sepharose and benzamidine-Sepharose *** revealed a main protein band of approximately 28 kDa on SDS-PAGE and was particularly inhibited by serine proteinase *** specificity analysis revealed that the enzyme specifically cleaved at the carboxyl side of arginine and lysine residues,suggesting the characteristic of a trypsin-type serine *** gene was cloned based on the N-terminal sequence and the conserved active site peptide of serine proteinases together with 5’-RACE and 3’-*** coding region gave an amino-acid sequence of 242 residues including the initiation methionine and a signal peptide of 20 *** acid residues of His,Aspand Serconsisting the catalytic triad of serine proteinases were conserved in the *** carp MBSP shared relatively high identities with other serine proteinases,especially in well-conserved regions.

关键词： Crucian carp Myofibril Serine proteinase cdna cloning

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Serum Inhibitor for the Trimeresurus Flavoviridis Venom Phos...

cloning of the cdna encoding adenosine 5'-monophosphate deaminase 1 and its mRNA expression in Japanese flounder Paralichthys olivaceus

“基因、进化与生理功能多样性”海内外学术研讨会暨中国生理学会第七届比较生理学学术会议

作者： Shu-Jing Li,Chun-Hua Yang,Qian-Ping Guo,Hui-Jian Wu~* Department of Bioscience and Biotechnology,Dalian University of Technology,Dalian 116024

The venom of Habu snake Trimeresurus flavovirids consists of several different isozymes of phospholipase A2(PLA2),and PLA-B is the isozyme that exhibits a characteristic physiological function of the edema. The protein inhibitor for this PLA-B was iso- lated from the serum of Habu *** PLA-B inhibitor was found to consist of three protein components designated asⅠ,Ⅱ,andⅢ,and it was found that each component per se is devoid of inhibitory activity,but they are active cooperatively with all three proteins. We purified the componentⅡby several different column *** properties of purified PLA2 inhibitor revealed a characteristic property of glycoproteins,the molecular weight of which was deduced from 25 kDa to 23 kDa by the treatment with N-glycanase. Determining the amino acid se- quences of N-terminal 70 residues and of C-terminal 20 residues by Edman degradation, the cdna cloning was performed for determination of the full *** present results have shown that serum inhibitor.

关键词： Inhibitor Phospholipase Purification cdna cloning

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Chinese Journal of Oceanology and Limnology 2013年第1期31卷 118-127页

作者：蒋克勇孙姝娟刘梅王宝杰孟晓林王雷 R&D Center of Marine Biotechnology Institute of OceanologyChinese Academy of Sciences Graduate University of Chinese Academy of Sciences

AMP deaminase catalyzes the conversion of AMP into IMP and ammonia. In the present study, a full-length cdna of AMPD1 from skeletal muscle of Japanese flounder Paralichthys olivaceus was cloned and characterized. The 2 526 bp cdna contains a 5'-UTR of 78 bp, a 3'-UTR of 237 bp and an open reading frame (ORF) of 2 211 bp, which encodes a protein of 736 amino acids. The predicted protein contains a highly conserved AMP deaminase motif (SLSTDDP) and an ATP-binding site sequence (EPLMEEYAIAAQVFK). Phylogenetic analysis showed that the AMPD1 and AMPD3 genes originate from the same branch, but are evolutionarily distant from the AMPD2 gene. RT-PCR showed that the flounder AMPD1 gene was expressed only in skeletal muscle. QRT-PCR analysis revealed a statistically significant 2.54 fold higher level of AMPD1 mRNA in adult muscle (750±40 g) compared with juvenile muscle (7.5±2 g) (P<0.05). HPLC analysis showed that the IMP content in adult muscle (3.35±0.21 mg/g) was also statistically significantly higher than in juvenile muscle (1.08±0.04 mg/g) (P<0.05). There is a direct relationship between the AMPD1 gene expression level and IMP content in the skeletal muscle of juvenile and adult flounders. These results may provide useful information for quality improvement and molecular breeding of aquatic animals.

关键词： AMPD1 cdna cloning mRNA expression IMP skeletal muscle Japanese flounder