秦浚川
生物化学与分子生物学
个性化签名
- 姓名:秦浚川
- 目前身份:
- 担任导师情况:
- 学位:
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学术头衔:
博士生导师
- 职称:-
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学科领域:
生物化学
- 研究兴趣:生物化学与分子生物学
秦浚川,男,1943年11月出生,1965年毕业于复旦大学生化专业,长期从事生物化学与分子生物学的教学与科研工作。曾主持武汉大学生化系生化教材的编写和生化实验室的创建。曾在美国堪萨斯大学生化系访问和从事博士后研究,主攻杆状病毒分子生物学。1991年作为骨干参加“昆虫病毒理论及应用基础研究”项目,获国家教委科技进步奖一等奖。1991年曾主持国家863项目1项,国家自然科学基金2项,省部级项目3项,建立了Sf9细胞和家蚕幼虫表达系统。“以杆状病毒表达系统为技术平台研究药用重组蛋白质”项目获2004年度江苏省科技进步奖一等奖。1993年起享受政府国务院特殊津贴。
现任“医学分子生物学杂志”及“中国生化制药杂志”编委,兼任南京农业大学农业部生化生理重点实验室、江苏省寄生虫分子生物学重点实验室学术委员会委员。
首次发现和报导了昆虫杆状病毒RNA的5'帽子结构,查明了苜蓿夜蛾核型多角体病毒的一个增强子(hr5)的序列及其附近的一个新的阅读框架和p10基因的启动区序列;首次应用系统缺失法证实了AcNPV的 p10基因启动子的核心保守序列是位于转录起点附近的TAAG盒,而与原先推测的TATA box无关;参加国家自然科学基金会《生物化学与分子生物学发展战略研究组》分工负责编写的《分子病毒学》专题调研报告,全面系统地反映了国内外分子病毒学的现状和发展趋势,提出了合理的对策;在国际上率先在昆虫细胞和家蚕表达系统中克隆表达和纯化了人M-CSF、GM-CSF、SCF、丁酰胆碱酯酶及对氧磷酶等11种有重要生理作用和药用价值的重组蛋白质;最早建立了用家蚕幼虫大规模制备rhM-CSF精品的中试工艺,并研究了rhM-CSF应用于升白血球抗真菌感染的动物实验。先后在国内外核心杂志上发表论文70多篇,其中SCI 25篇,合编专著1本,获国家发明专利证书2项,另申请国家发明专利2项。
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主页访问
1385
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成果阅读
356
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成果数
7
秦浚川, QIN JUN-CHUAN† AND ROBERT F. WEAVER*
JOURNAL OF VIROLOGY, July 1982, p. 234-240,-0001,():
-1年11月30日
Viral RNA from fall armyworm (Spodoptera frugiperda) cells infected with Autographa californica nuclear polyhedrosis virus contains cap structures. Most of the cap labeled in vivo with [3H]methionine or 32pI cochromatographed on DEAE-cellulose with the -5 charge marker; a minor com onent appeared at -4 net charge. The former is probably a cap 1 structure (m GpppXmYp), and the latter is probably a cap 0 (m7GpppXp). On the basis of relative labeling of the two caps with [3H]adenosine and [H]guanosine, we concluded that each cap contained at least one adenosine residue in addition to guanosine and, therefore, that cap 0 contained m7GpppAp. Cleavage of [3H]methionine-labeled viral RNA with tobacco acid pyrophosphatase released a labeled component that cochromatographed on polyethyleneimine-cellulose with m7Gp, confirming the m7GpppX linkage in the cap. These results were also seen with host polyadenylated RNA. The caps appeared in nearly equal abundance in viral polyadenylated and nonpolyadenylated RNAs. The ratio of 32p; incorporated into the cap to that incorporated into mononucleotides suggested average lengths for the polyadenylated and non-polyadenylated RNAs of 1,800 and 1,200 nucleotides, respectively.
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秦浚川, By AIFU LIU, †, JUNCHUAN QIN, ‡, CAROLYN RANKIN, STEVEN E. HARDIN AND ROBERT F. WEAVER*
J. gen. Virol. (1986), 67, 2565-2570.,-0001,():
-1年11月30日
The nucleotide sequence of a 1587 bp region lying within the HindIII-Q fragment of Autographa californica multiple nucleocapsid nuclear polyhedrosis virus (AcMNPV) DNA has been determined. It begins in the EcoRI-S-EcoRI-X region, continues to the HindlII-P/Q boundary and contains an open reading frame that codes for a polypeptide of 240 amino acids (p26). This open reading frame is also included in the 1100 and 1500 base transcripts previously mapped to this region. The sequence reveals that the 5' ends of the 1100 and 1500 base transcripts are located 20 bp downstream from the end of a putative TATA box (TAATTAAAT) and 19bp upstream from thetranslation start codon (ATG) of the p26 open reading frame. The translation termination codon (TAA) falls in the immediate 5' flanking region of the major late p 10 gene of AcMNPV, 3bp downstream from the putative TATA box. The probable polyadenylation site for the 1100 base transcript lies 23bp downstream from the cap site for the 750 and 2500 base transcripts encoding the pl0 protein. The 5' flanking region of the p26 open reading frame contains the EcoRI site-rich region, hr5, whose sequence is included here. The EcoRI site-rich region, hrs, consists of six imperfect tandem repeats of a sequence that includes the EcoRI recognition site. These direct repeats also include many inverted repeats.
AcMNPV/, open reading frame/, hrs/, nucleotide sequence
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秦浚川, Wan-Li Wei, *, Jun-Chuan Qin† and Man-Ji Sun*‡
BIOCHEM PHARMACOL 60; 1: 121-126,-0001,():
-1年11月30日
The human butyrylcholinesterase (BChE, EC 3.1.1.8) gene was highly expressed in Bombyx mori using baculovirus vector, and the biochemical-pharmacological properties of its product were studied. BChE cDNA was cloned into transfer vector pBn96 and co-transfected with wild-type Bombyx mori nucleopolyhedrovirus (BmNPV) DNA into BmN cells. The recombinant virus with the highest enzyme activity was sorted out and purified. Once the BmN cells or silkworm larvae had been infected with the recombinant virus, recombinant human BChE (rhBChE) could be secreted into the culture medium or the hemolymph of the larvae at levels of 1.5mg•L-1 and 35mg•L-1, respectively. Western blot and enzymatic staining of the electrophoresis gel of non-denatured protein showed that rhBChE manifested similar antigenicity and enzyme activity to native human BChE (nhBChE). The production of rhBChE in the hemolymph was 23-fold higher than that in BmN cells and about 280-fold that in Chinese hamster overy cells (125μmg•L-1). This is the first report of human BChE expression in silkworm with the highest level of yield so far. rhBChE was highly similar to nhBChE in respect to substrate affinity, inhibitor sensitivity, and reactivity of the inhibited enzyme. It is suggested that rhBChE functions as well as nhBChE and has potential practical value.
butyrylcholinesterase, gene expression, baculovirus, Bombyx mori, sarin
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【期刊论文】Expression of a novel recombinant dual human stem cell factor in insect cells
秦浚川, Junhai Han, a, Xiaohui Yan, Jie Zhu, Xiaoyong Zhi, Yuhui Zang, Beifen Shen, b and Junchuan Qin a, *
Protein Expression and Purification 31(2003)311-317,-0001,():
-1年11月30日
Stem cell factor (SCF) is a hematopoietic cytokine that promotes the survival, proliferation, and differentiation of hematopoietic cells. A dual human stem cell factor (dhSCF) cDNA was constructed, which consisted of a full-length human stem cell factor cDNA plus a truncated hSCF cDNA (1-145aa), linked by a peptide (GGGGSGGGGSGG) coding region. The dhSCF gene was cloned into baculovirus transfer vector pAcSecG2T under the control of polyhedrin promoter. The Sf9 cells infected with the recombinant virus expressed rdhSCF up to 6000 U/106 cell in flask and 8300 U/106 cell in spinner flask. The rdhSCF was purified by two-step chromatography. The molecular mass of rdhSCF was examined by western blotting and HPLC analysis. The specific activity of rdhSCF was up to 3.1
Dual human stem cell factor, Insect expression system, Sf9 cell, pAcSecG2T
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秦浚川, Tao Chen, Yuhui Zang, Jie Zhu, Haiqin Lu, Junhai Han, Junchuan Qin*
Protein Expression and PuriWcation 41(2005)402-408,-0001,():
-1年11月30日
A novel human stem cell factor (SCF)/macrophage colony-stimulating factor (M-CSF) fusion protein gene was constructed, in which the coding regions of human SCF cDNA (1-165aa) and the truncated M-CSF cDNA (1-149aa) were connected by a linker sequence encoding a short peptide GGGGSGGGGSGG. The SCF/M-CSF gene was cloned into baculovirus transfer vector pVL1392 under the control of polyhedrin promoter and expressed in the Sf9 cells (Spodoptera frugiperda). SDS–PAGE and Western blot analysis showed that the puriWed fusion protein was a homodimer with a molecular weight about 84kDa under non-reducing conditions or a monomer about 42kDa under reducing conditions. The speciWc activity of rhSCF/M-CSF was 17 times as high as that of monomeric rhSCF to stimulate the proliferation of TF-1 cell. The results of macrophages colony-forming (CFU-M) assay performed with human bone marrow mononuclear cells demonstrated that rhSCF/M-CSF was more potent in promoting CFU-M than the equimolar of SCF, M-CSF or that of two cytokines mixture.
SCF, M-CSF, Fusion protein, Expression in insect cell
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【期刊论文】Expression, refolding, and characterization of a novel recombinant dual human stem cell factor
秦浚川, Haiqin Lu, Yuhui Zang, Yuguan Ze, Jie Zhu, Tao Chen, Junhai Han, Junchuan Qin*
Protein Expression and PuriWcation 43(2005)126-132,-0001,():
-1年11月30日
A novel recombinant dual human stem cell factor (rdhSCF) gene which consisted of a full-length hSCF(1-165 aa) cDNA and atruncated hSCF (1-145 aa) cDNA, linked by a peptide (GGGGSGGGGSGG) coding region, was constructed and cloned into Escherichia coli expression vector pET-22b. The rdhSCF was expressed at high level in E. coli BL21(DE3) and existed mainly as inclusion bodies. The inclusion bodies were solubilized in urea and refolded by ion-exchange chromatography. After renaturation, the purity of the yielded rdhSCF was up to 90%. Cell proliferation assay showed that the speciWc activity of the rdhSCF was 2.86
Dual human stem cell factor, pET-22b, Refolding, Escherichia coli expression system, BL21(, DE3),
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秦浚川, Haiqin Lu, Jie Zhu, Yuhui Zang, Yuguan Ze, Junchuan Qin*
Biochemical Pharmacology 70(2005)1019-1025,-0001,():
-1年11月30日
Human paraoxnase-3 (hPON3) (EC3.1.8.1) is a lipid-associated enzyme with antioxidant activity, and can inhibit the oxidation of lowdensity lipoprotein (LDL), thereby inhibiting early atherogenic process. In the present study, human PON3 gene was cloned from Human Fetal Liver Marathon-Ready cDNA and expressed in insect cells using baculovirus vector. Twenty-eight milligrams of purified recombinant hPON3 (rhPON3) was obtained from 1 L Sf9 cells culture. The Km and Vmax values of rhPON3, with respective to phenylacetate hydrolysis were 7.46
Human paraoxonase-3, Baculovirus-mediated expression system, Sf9 cell, Gene expression, LDL oxidation, Dihydrocoumarin
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