Investigation on the interaction between SSAO, its substrate and the inhibitor using bio-functionalized chromatography

Hong Li; Feng Qu; Jian Dong Xu; Yu Lin Deng

Investigation on the interaction between SSAO, its substrate and the inhibitor using bio-functionalized chromatography

Hong Li^*
, Feng Qu
, Jian Dong Xu
, Yu Lin Deng

^*此作品的通讯作者

医学科学与工程学院

Beijing Institute of Technology

科研成果: 期刊稿件 › 文章 › 同行评审

摘要

Bio-functionalized chromatography-capillary electrophoresis was used in investigating the interaction between semicarbazide-sensitive amine oxidase(SSAO), its substrate benzylamine as well as its inhibitor 2-BrEA. SSAO activity detection showed that SSAO could keep 70%∼85% activity of its free form after being immobilized onto liposome. The active immobilized SSAO was added to the PBS. With the increase of the immobilized enzyme concentration, the effective mobility of its specific substrate, benzylamine, decreased from 4.06×10^-4 cm²·V^-1·s^-1 to 0.81×10^-4cm² · V^-1 · s^-1 at pH=5, and from 3.91 × 10^-4cm² · V^-1 · s^-1 to 0.29 × 10^-4cm² · V^-1 · s^-1 at pH=7. If the concentration of the inhibitor 2-BrEA in the buffer was increased from 10^-6 mol · L^-1 to 10^-1 mol · L^-1, the effective mobility of benzylamine would increase from 1.42 × 10^-4cm² · V^-1 · s^-1 to 2.22 × 10^-4cm² · V^-1 · s^-1.

源语言	英语
页（从-至）	1117-1121
页数	5
期刊	Beijing Ligong Daxue Xuebao/Transaction of Beijing Institute of Technology
卷	28
期	12
出版状态	已出版 - 12月 2008

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@article{5b009c67c4bd47deb73cea553f477adb,

title = "Investigation on the interaction between SSAO, its substrate and the inhibitor using bio-functionalized chromatography",

abstract = "Bio-functionalized chromatography-capillary electrophoresis was used in investigating the interaction between semicarbazide-sensitive amine oxidase(SSAO), its substrate benzylamine as well as its inhibitor 2-BrEA. SSAO activity detection showed that SSAO could keep 70\%∼85\% activity of its free form after being immobilized onto liposome. The active immobilized SSAO was added to the PBS. With the increase of the immobilized enzyme concentration, the effective mobility of its specific substrate, benzylamine, decreased from 4.06{\texttimes}10-4 cm2·V-1·s-1 to 0.81{\texttimes}10-4cm2 · V-1 · s-1 at pH=5, and from 3.91 {\texttimes} 10-4cm2 · V-1 · s-1 to 0.29 {\texttimes} 10-4cm2 · V-1 · s-1 at pH=7. If the concentration of the inhibitor 2-BrEA in the buffer was increased from 10-6 mol · L-1 to 10-1 mol · L-1, the effective mobility of benzylamine would increase from 1.42 {\texttimes} 10-4cm2 · V-1 · s-1 to 2.22 {\texttimes} 10-4cm2 · V-1 · s-1.",

keywords = "2-BrEA, Benzylamine, Bio-functionalized chromatography, Capillary electrophoresis, Liposome, SSAO",

author = "Hong Li and Feng Qu and Xu, \{Jian Dong\} and Deng, \{Yu Lin\}",

year = "2008",

month = dec,

language = "English",

volume = "28",

pages = "1117--1121",

journal = "Beijing Ligong Daxue Xuebao/Transaction of Beijing Institute of Technology",

issn = "1001-0645",

publisher = "Beijing Institute of Technology",

number = "12",

}

TY - JOUR

T1 - Investigation on the interaction between SSAO, its substrate and the inhibitor using bio-functionalized chromatography

AU - Li, Hong

AU - Qu, Feng

AU - Xu, Jian Dong

AU - Deng, Yu Lin

PY - 2008/12

Y1 - 2008/12

N2 - Bio-functionalized chromatography-capillary electrophoresis was used in investigating the interaction between semicarbazide-sensitive amine oxidase(SSAO), its substrate benzylamine as well as its inhibitor 2-BrEA. SSAO activity detection showed that SSAO could keep 70%∼85% activity of its free form after being immobilized onto liposome. The active immobilized SSAO was added to the PBS. With the increase of the immobilized enzyme concentration, the effective mobility of its specific substrate, benzylamine, decreased from 4.06×10-4 cm2·V-1·s-1 to 0.81×10-4cm2 · V-1 · s-1 at pH=5, and from 3.91 × 10-4cm2 · V-1 · s-1 to 0.29 × 10-4cm2 · V-1 · s-1 at pH=7. If the concentration of the inhibitor 2-BrEA in the buffer was increased from 10-6 mol · L-1 to 10-1 mol · L-1, the effective mobility of benzylamine would increase from 1.42 × 10-4cm2 · V-1 · s-1 to 2.22 × 10-4cm2 · V-1 · s-1.

AB - Bio-functionalized chromatography-capillary electrophoresis was used in investigating the interaction between semicarbazide-sensitive amine oxidase(SSAO), its substrate benzylamine as well as its inhibitor 2-BrEA. SSAO activity detection showed that SSAO could keep 70%∼85% activity of its free form after being immobilized onto liposome. The active immobilized SSAO was added to the PBS. With the increase of the immobilized enzyme concentration, the effective mobility of its specific substrate, benzylamine, decreased from 4.06×10-4 cm2·V-1·s-1 to 0.81×10-4cm2 · V-1 · s-1 at pH=5, and from 3.91 × 10-4cm2 · V-1 · s-1 to 0.29 × 10-4cm2 · V-1 · s-1 at pH=7. If the concentration of the inhibitor 2-BrEA in the buffer was increased from 10-6 mol · L-1 to 10-1 mol · L-1, the effective mobility of benzylamine would increase from 1.42 × 10-4cm2 · V-1 · s-1 to 2.22 × 10-4cm2 · V-1 · s-1.

KW - 2-BrEA

KW - Benzylamine

KW - Bio-functionalized chromatography

KW - Capillary electrophoresis

KW - Liposome

KW - SSAO

UR - https://www.scopus.com/pages/publications/58249089326

M3 - Article

AN - SCOPUS:58249089326

SN - 1001-0645

VL - 28

SP - 1117

EP - 1121

JO - Beijing Ligong Daxue Xuebao/Transaction of Beijing Institute of Technology

JF - Beijing Ligong Daxue Xuebao/Transaction of Beijing Institute of Technology

IS - 12

ER -

Investigation on the interaction between SSAO, its substrate and the inhibitor using bio-functionalized chromatography

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