兔血浆SSAO的分离纯化及其酶动力学研究
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摘要
背景与目的:血浆中含有氨基脲敏感型胺氧化酶(semicarbazide-sensitive amine oxidase,SSAO)。本研究的目的是纯化兔血浆中的SSAO蛋白,并以甲胺为底物研究兔血浆中具有SSAO酶活性的蛋白组分的酶动力学参数。材料与方法:利用DEAE-琼脂糖FF凝胶柱层析分离兔血浆蛋白,测定各收集组分的SSAO酶活性;以甲胺为底物测定SSAO酶动力学参数。结果:从兔血浆蛋白中分离得到两个具有SSAO酶活性的蛋白组分A和B。以甲胺为底物,未处理的血浆SSAO的酶动力学参数Km=1.83±0.13 mmol/L,Vmax=0.12±0.003 nmol/min/mg。蛋白组分B的酶动力学参数Km值(2.05±0.43 mmol/L)小于蛋白组分A的Km值(3.14±0.63 mmol/L)。组分B的酶动力学参数Vmax值(1.46±0.10 nmol/min/mg)小于组分A的Vmax值(2.85±0.20 nmol/min/mg)。结论:兔血浆含有两种SSAO酶组分,均可以催化甲胺氧化脱氨生成甲醛;组分A、B动力学特征有所不同。
BACKGROUND AND AIM: To purify and investigate enzyme kinetic properties of rabbit plasma semicarbazide-sensitive amine oxidases (SSAO), using methylamine as substrate. MATERIALS AND METHODS: Formaldehyde, an oxidative deamination product of methylamine, was examined by HPLC analysis. Rabbit plasma SSAO was purified by chromatography with DEDE-sepharose FF (eluted with 30 mmol/L and then 100 mmol/L sodium phosphate buffers, all at pH 7.0), then assayed and Michaelis-Menten analyzed. RESULTS: Two kinds of SSAOs (labeled as peak A and peak B) had been obtained, which were catalytically active with methylamine as substrate. The kinetic parameters Km and Vmax of plasma were 1.83±0.13 mmol/L and 22.20±0.48 nmol/min/mg, respectively. The Km of peak B (2.05±0.43 mmol/L) was lower than that of peak A (3.14±0.63 mmol/L), the Vmax of the peak A (1.03±0.07 nmol/min/mg) was lower than that of peak B (2.52±0.17 nmol/min/mg). CONCLUSION: In rabbit plasma, there are two kinds of SSAO which can catalyze methylamine into formaldehyde and have significantly different kinetic parameters.
BACKGROUND AND AIM: To purify and investigate enzyme kinetic properties of rabbit plasma semicarbazide-sensitive amine oxidases (SSAO), using methylamine as substrate. MATERIALS AND METHODS: Formaldehyde, an oxidative deamination product of methylamine, was examined by HPLC analysis. Rabbit plasma SSAO was purified by chromatography with DEDE-sepharose FF (eluted with 30 mmol/L and then 100 mmol/L sodium phosphate buffers, all at pH 7.0), then assayed and Michaelis-Menten analyzed. RESULTS: Two kinds of SSAOs (labeled as peak A and peak B) had been obtained, which were catalytically active with methylamine as substrate. The kinetic parameters Km and Vmax of plasma were 1.83±0.13 mmol/L and 22.20±0.48 nmol/min/mg, respectively. The Km of peak B (2.05±0.43 mmol/L) was lower than that of peak A (3.14±0.63 mmol/L), the Vmax of the peak A (1.03±0.07 nmol/min/mg) was lower than that of peak B (2.52±0.17 nmol/min/mg). CONCLUSION: In rabbit plasma, there are two kinds of SSAO which can catalyze methylamine into formaldehyde and have significantly different kinetic parameters.
引文
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[9] Lizcano JM, Escrich E, Ribalta T, Muntane J and Unzeta M. Amine oxidase activities in rat breast cancers induced experimentally with 7,12-dimethylbenz(alpha)anthracene. Biochem Pharmacol, 1991b, 42: 263–9.
[10]叶静,刘协和.氧化应激与Alzheimer病.自由基生命科学进展. 2001, 8: 87-91
[11]丛杰,方允中.应激反应引起氧化损伤.自由基生命科学进展. 1993, 1: 28-34
[12]任玲,今春明,邓玉林. SSAO酶活性的测定方法研究.生命科学仪器, 2004, 2(1): 28-31
[13] Lizcano JM, Tipton KF, Unzeta M. Purification and characterization of membrane-bound semicarbazide-sensitive amine oxidase from bovine lung [J]. Biochem. J, 1998, 331: 69–78.
[14] Coleman AA, Scaman CH, Kang YJ, et al. Stereochemical trends in copper amine oxidase reactions [J]. J Biol Chem, 1991, 266 (11): 6795-6800.
[15] Falk MC, Staton AJ,Williams TJ. Heterogeneity of pig plasma amine oxidase molecular and catalytic properties of chromatographically isolated forms [J]. Biochem J, 1983, 22: 3746-3751.
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[19] Li H, Luo WH, Lin JX, et al. Assay of plasma semicarbazide-sensitive amine oxidase and determination of its endogenous substrate methylamine by liquid chromatography [J]. J Chromatogr, B, 2004, 810(2): 277-282.
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[21] Luo WH, Li H, Zhang Y, et al. Determination of formaldehyde in blood plasma by high-performance liquid chromatography with fluorescence detection [J]. J Chromatogr. B, 2001, 753(2): 253-257.
[22] Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding [J]. Anal. Biochem., 1976, 72: 248-254
[23]张美,李慧,罗红军.脂多糖诱导急性肺损伤过程中SSAO酶的活性变化[J].癌变畸变突变, 2007, 19(3): 223-226.
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[25] Falk MC, Staton AJ,Williams TJ. Heterogeneity of pig plasma amine oxidase molecular and catalytic properties of chromatographically isolated forms [J]. Biochem J, 1983, 22: 3746-3751.
[26] Lizcano JM, Tipton KF, Unzeta M. Time-dependent activation of the SSAO from ox lung microsomes [J]. Biochem. J, 2000, 351: 789–794.
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[8] Lizcano JM, Balsa D, Tipton KF and Unzeta M. The oxidation of dopamine by the semicarbazide-sensitive amine oxidase (SSAO) from rat vas deferens. Biochem Pharmacol, 1991a, 41: 1107–10.
[9] Lizcano JM, Escrich E, Ribalta T, Muntane J and Unzeta M. Amine oxidase activities in rat breast cancers induced experimentally with 7,12-dimethylbenz(alpha)anthracene. Biochem Pharmacol, 1991b, 42: 263–9.
[10]叶静,刘协和.氧化应激与Alzheimer病.自由基生命科学进展. 2001, 8: 87-91
[11]丛杰,方允中.应激反应引起氧化损伤.自由基生命科学进展. 1993, 1: 28-34
[12]任玲,今春明,邓玉林. SSAO酶活性的测定方法研究.生命科学仪器, 2004, 2(1): 28-31
[13] Lizcano JM, Tipton KF, Unzeta M. Purification and characterization of membrane-bound semicarbazide-sensitive amine oxidase from bovine lung [J]. Biochem. J, 1998, 331: 69–78.
[14] Coleman AA, Scaman CH, Kang YJ, et al. Stereochemical trends in copper amine oxidase reactions [J]. J Biol Chem, 1991, 266 (11): 6795-6800.
[15] Falk MC, Staton AJ,Williams TJ. Heterogeneity of pig plasma amine oxidase molecular and catalytic properties of chromatographically isolated forms [J]. Biochem J, 1983, 22: 3746-3751.
[16] Lizcano JM, Tipton KF, Unzeta M. Time-dependent activation of the SSAO from ox lung microsomes [J]. Biochem. J, 2000, 351: 789–794.
[17] Hartman, CH and Klinman, JP. Structure-Function studies of substrate oxidation by bovine serum amineoxidase: relationship to cofactor structure and mechanism [J]. Biochem J, 1991, 30: 4605-4611.
[18] Lizcano JM, Tipton KF, Unzeta M. Purification and characterization of membrane-bound semicarbazide-sensitive amine oxidase from bovine lung [J]. Biochem. J, 1998, 331: 69–78.
[19] Li H, Luo WH, Lin JX, et al. Assay of plasma semicarbazide-sensitive amine oxidase and determination of its endogenous substrate methylamine by liquid chromatography [J]. J Chromatogr, B, 2004, 810(2): 277-282.
[20] Lizcano JM, Tipton KF, Unzeta M. Purification and characterization of membrane-bound semicarbazide-sensitive amine oxidase (SSAO) from bovine lung. Biochem J. 1998, 331: 69–78.
[21] Luo WH, Li H, Zhang Y, et al. Determination of formaldehyde in blood plasma by high-performance liquid chromatography with fluorescence detection [J]. J Chromatogr. B, 2001, 753(2): 253-257.
[22] Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding [J]. Anal. Biochem., 1976, 72: 248-254
[23]张美,李慧,罗红军.脂多糖诱导急性肺损伤过程中SSAO酶的活性变化[J].癌变畸变突变, 2007, 19(3): 223-226.
[24] Vidrio H, Medina M. Hypotensive effect of hydroxylamine, an endogenous nitric oxide donor and SSAO inhibitor [J]. 2007, 114(6): 863-5.
[25] Falk MC, Staton AJ,Williams TJ. Heterogeneity of pig plasma amine oxidase molecular and catalytic properties of chromatographically isolated forms [J]. Biochem J, 1983, 22: 3746-3751.
[26] Lizcano JM, Tipton KF, Unzeta M. Time-dependent activation of the SSAO from ox lung microsomes [J]. Biochem. J, 2000, 351: 789–794.
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