陈清西
主要研究方向:酶的结构与功能、酶作用动力学、抑制动力学、失活动力学、激活动力学、酶活力调控机理、抑制作用机理;酶产品及酶抑制剂的开发应用;蛋白质折叠与去折叠;抗癌多肽;癌变机理;蛋白质组学。
个性化签名
- 姓名:陈清西
- 目前身份:
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学术头衔:
博士生导师, 教育部“新世纪优秀人才支持计划”入选者
- 职称:-
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学科领域:
生物化学
- 研究兴趣:主要研究方向:酶的结构与功能、酶作用动力学、抑制动力学、失活动力学、激活动力学、酶活力调控机理、抑制作用机理;酶产品及酶抑制剂的开发应用;蛋白质折叠与去折叠;抗癌多肽;癌变机理;蛋白质组学。
陈清西,教授,博士生导师。1985年1月毕业于厦大生物系生化专业,获硕士学位,1999年7月毕业并获得清华大学理学博士学位。2000年1月至2002年2月在美国加州Berkeley大学工作2年。
现任厦门大学生命科学院生化与分子生物学研究所所长。厦门大学生命科学学院学术委员会、学位委员会成员;中国生物化学与分子生物学学会蛋白质专业学术委员会委员;酶学专业学生委员会委员;中国农业生物化学与分子生物学理事;福建省生物化学与分子生物学学会副理事长;厦门市农业学会常务理事;《厦门大学学报(自然科学版)》、《中国生物化学与分子生物学学报》编委;福建省重点学科“生化与分子生物学”学术带头人。2003年入选教育部跨世纪人才.主要从事分子酶学机理及其应用的研究。
主要研究方向:酶的结构与功能、酶作用动力学、抑制动力学、失活动力学、激活动力学、酶活力调控机理、抑制作用机理;酶产品及酶抑制剂的开发应用;蛋白质折叠与去折叠;抗癌多肽;癌变机理;蛋白质组学。研究成果:项目“锯缘青蟹碱性磷酸酶活力调控的分子机理研究”获得2002年教育部提名国家科技奖-自然科学二等奖;“养殖环境污染对长毛对虾磷酸酯酶活力的影响” 获得2003年度福建省科学技术进步奖三等奖;研究论文曾获得2003年和2006年福建省自然科学优秀论文二等奖。发表研究论文170多篇,其中在国际SCI源学术刊物发表65篇。
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509
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成果数
9
陈清西, Bo Leng, Xiao-Dan Liu, Qing-Xi Chen*
FEBS Letters 579(2005)1187-1190,-0001,():
-1年11月30日
An anti-cancer peptide was purified from the Mercenaria (Meretrix meretrix Linnaeus) by the method of chromatography on Sephadex G-25 and FPLC, and its molecular weight was determined to be 3147 Da by the way of MALDITOF mass spectrum. The effects of this peptide on human gastric gland carcinoma cells (BGC-823) and their cytoskeletal morphology were investigated. The results showed that the peptide could inhibit the proliferation of BGC-823 cells and obviously destroy the skeletal structures of the cells. When the concentration of the peptide reached 4.0μg/ml, the inhibition percentage of the cell growth was about 60%. The effects of this anticancer peptide on the activities of superoxide dismutase (SOD), alkaline phosphatase (ALP) and tyrosinase were studied. The results showed that the peptide activated ALP and SOD, but inhibit the tyrosinase activity. When the concentration of the peptide reached to 0.5μg/ml, the relative activities of SOD, ALP and tyrosinase were determined to be 188.5%, 122.0% and 27.5%, respectively.
Anticancer peptide, Human gastric gland carcinoma cell, Superoxidedismutase, Alkaline phosphatase, Tyrosinase, Effect, Meretrix meretrix Linnaeus
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陈清西, Qing-Xi Chen a, *, Zhe Zhang a, Huang Huang a, Fu-Kun Zhao b, Gen-Jun Xu b
The International Journal of Biochemistry & Cell Biology 35(2003)1227-1233,-0001,():
-1年11月30日
Changes of activity and conformation of Ampullarium crossean-glucosidase in different concentrations of guanidine hydrochloride (GuHCl) have been studied by measuring the fluorescence spectra and its relative activity after denaturation. The fluorescence intensity of the enzyme decreased distinctly with increasing guanidine concentrations, the emission peaks appeared red shifted (from 338.4 to 350.8nm), whereas a new fluorescence emission peak appeared near 310nm. Changes in the conformation and catalytic activity of the enzyme were compared. A corresponding rapid decrease in catalytic activity of the enzyme was also observed. The extent of inactivation was greater than that of conformational changes, indicating that the active site of the enzyme is more flexible than the whole enzyme molecule. k+0>kβ+0 also showed that the enzyme was protected by substrate to a certain extent during guanidine denaturation.
β-Glucosidase, Denaturation, Inactivation, Kinetics, Guanidine hydrochloride
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【期刊论文】E-ect of metal ions on the activity of green crab (Scylla serrata) alkaline phosphatase
陈清西, Qing-Xi Chen a, Wen-Zhu Zheng a, Jing-Yu Lin a, Yan Shi a, Wen-Zhang Xie b, Hai-Meng Zhou b, *
The International Journal of Biochemistry & Cell Biology 32(2000)879-885,-0001,():
-1年11月30日
Green crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme, which catalyzes the nonspeci
Alkaline phosphatase, Green crab, Metalion, Inhibition, Activation, Kinetic model
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陈清西, Ling Qiu, Qing-Xi Chen, *, Qin Wang, Hao Huang and Kang-Kang Song
Bioorganic & Medicinal Chemistry 13(2005)6206-6211,-0001,():
-1年11月30日
3,5-Dihydroxyphenyl decanoate (DPD) is found to inhibit the diphenolase activity of tyrosinase from mushroom (Agaricus bisporus). The effects of DPD on the diphenolase activity of mushroom tyrosinase have been studied. The results show that the enzyme activity decreases very slowly with an increase in DPD concentrations at lower concentrations of DPD (between 5 and 60μM). But at higher concentrations of DPD, DPD can strongly inhibit the diphenolase activity of the enzyme and the inhibition is irreversible. The IC50 value was estimated to be 96.5 lM. The inhibition mechanism of DPD has been investigated and the results show that DPD can bind to the free enzyme molecule and enzyme-substrate complex and lose the enzyme activity completely. The inhibition kinetics has been studied in detail by using the kinetic method of the substrate reaction described by Tsou. The microscopic rate constants of the enzyme inhibited by DPD at higher concentrations have been determined.
Mushroom tyrosinase, 3,, 5-Dihydroxyphenyl decanoate, Inhibition, Mechanism, Kinetics.,
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【期刊论文】Inhibitory effects on mushroom tyrosinase by p-alkoxybenzoic acids
陈清西, Qing-Xi Chen*, Kang-Kang Song, Ling Qiu, Xiao-Dan Liu, Huang Huang, Hua-Yun Guo
Food Chemistry 91(2005)269-274,-0001,():
-1年11月30日
The inhibitory kinetics of the diphenolase of mushroom tyrosinase by seven p-alkoxybenzoic acids has been studied. The results show that these derivatives of benzoic acid behave as reversible inhibitors. Among them, p-hydroxybenzoic acid is competitive, while p-methoxybenzoic acid is non-competitive, p-ethoxybenzoic acid is mixed-II type, and the rest all behave as classical uncompetitive inhibitors. The inhibition constants of all of the seven compounds assayed, characterizing the inhibition, were evaluated. The models of the interactions between the enzyme and the inhibitors are compared.
Mushroom tyrosinase, Diphenolase, p-alkoxybenzoic acid, Inhibitory mechanism
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陈清西, Yan Shi, Qing-Xi Chen*, Qin Wang, Kang-Kang Song, Ling Qiu
Food Chemistry 92(2005)707-712,-0001,():
-1年11月30日
The effects of cinnamic acid and its derivatives (2-hydroxycinnamic acid, 4-hydroxycinnamic acid and 4-methoxycinnamic acid) on the activity of mushroom tyrosinase have been studied. Results showed that cinnamic acid, 4-hydroxycinnamic acid and 4-methoxycinnamic acid strongly inhibited the diphenolase activity of mushroom tyrosinase and the inhibition was reversible. The IC50 values were estimated to be 2.10, 0.50 and 0.42mM, respectively. 2-Hydroxycinnamic acid had no inhibitory effect on the diphenolase activity of the enzyme. Kinetic analyses showed that the inhibition type of cinnamic acid and 4-methoxycinnamic acid was noncompetitive with the constants (KI) determined to be 1.994 and 0.458mM, respectively. The inhibition type of 4-hydroxycinnamic acid was competitive, with the inhibition constant (KI) was 0.244mM.
Mushroom tyrosinase, Diphenolase activity, Cinnamic acid and its derivatives, Inhibition kinetics
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陈清西, Qin Wang, Qing Xi Chen*, Xiao Hong Huang, Li-Na Ke, Yan Shi, and Jun Wang
Biochemistry (Moscow), Vol.69, No.8, 2004, pp. 918-920.,-0001,():
-1年11月30日
Polyphenol oxidase (EC 1.14.18.1) was purified from the pupae of blowfly (Sarcophaga bullata) by a procedure involving ammonium sulfate fractionation and chromatography on DEAE-cellulose and Sephadex G-100. Kinetic charac-teristics of the enzyme were determined using L-DOPA as substrate. The specific activity of the enzyme was 770 U/mg, and the Michaelis constant (Km) was 1.5±0.1mM (pH6.8, 30℃). Activity was maximal at 40℃, pH 6.5. Chemical modifica-tion experiments demonstrated that cysteine and tryptophan residues are essential and arginine residues are not essential to the enzyme function. The enzyme is inhibited by quercetin with an IC50 of 0.20±0.06mM. The inhibition is of competitive type, and the inhibition constant was determined to be 88 μM.
polyphenol oxidase, blowfly pupae, kinetic characterization, chemical modification
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陈清西, Xiao-Lan Xie, , Qing-Xi Chen, Min Gong, Qin Wang, and Yan Shi
The Protein Journal, Vol. 24, No. 5, July 2005,-0001,():
-1年11月30日
The effects of guanidinium chloride (GuHCl) on the activity of Penaeus vannamei b-N-acetyl-D-glucosaminidase (NAGase) have been studied. The results show that GuHCl, at appropriate concentrations, can lead to reversible inactivation of the enzyme, and the IC50 is estimated to be 0.6 M. Changes of activity and conformation of the enzyme in different concentrations of GuHCl have been studied by measuring the fluorescence spectra and its relative activity after denaturation. The fluorescence intensity of the enzyme decreases distinctly with increasing GuHCl concentrations, and the emission peaks appear red-shifted (from 339.4 to 360nm). Changes in the conformation and catalytic activity of the enzyme are compared. The extent of inactivation is greater than that of conformational changes, indicating that the active site of the enzyme is more flexible than the whole enzyme molecule. The kinetics of inactivation has been studied using the kinetic method of the substrate reaction. The rate constants of inactivation have been determined. The value of k+0 is larger than that of k+0? which suggests that the enzyme is protected by substrate to a certain extent during guanidine denaturation.
b-N-acetyl-D-glucosaminidase, denaturation, guanidinium chloride, inactivation kinetics, Penaeus vannamei.,
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陈清西, Qing-Xi Chen, , Li-Na Ke, Kang-Kang Song, Huang Huang, and Xiao-Dan Liu
The Protein Journal, Vol. 23, No. 2, February 2004,-0001,():
-1年11月30日
The effects of hexylresorcinol and dodecylresorcinol on the monophenolase and diphenolase activity of mushroom tyrosinase have been studied. The results show that hexylresorcinol and dodecylresorcinol can inhibit both monophenolase and diphenolase activity of the enzyme. The lag period of the enzyme was obviously lengthened, and the steady-state activity of the enzyme decreased sharply. Two μM of hexylresorcinol and dodecylresorcinol can lengthen the lag period from 98s to 260 and 275s, respectively. Both hexylresorcinol and dodecylresorcinol can lead to reversible inhibition of the enzyme. The IC50 values of hexylresorcinol and dodecylresorcinol were estimated as 1.24 and 1.15 μM for monophenolase and as 0.85 and 0.80μM for diphenolase, respectively. A kinetic analysis shows that hexylresorcinol and dodecylresorcinol are competitive inhibitors. The apparent inhibition constant for hexylresorcinol and dodecylresorcinol binding with free enzyme has been determined to be 0.443 and 0.405 μM for diphenolase, respectively.
Diphenolase, dodecylresorcinol, hexylresorcinol, inhibition, monophenolase, mushroom tyrosinase.,
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