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

^*Corresponding author for this work

School of Medical and Technology

Beijing Institute of Technology

Research output: Contribution to journal › Article › peer-review

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 4.06×10^-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.

Original language	English
Pages (from-to)	1117-1121
Number of pages	5
Journal	Beijing Ligong Daxue Xuebao/Transaction of Beijing Institute of Technology
Volume	28
Issue number	12
Publication status	Published - Dec 2008

Keywords

2-BrEA
Benzylamine
Bio-functionalized chromatography
Capillary electrophoresis
Liposome
SSAO

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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 4.06×10-4 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.",

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",

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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

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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

Abstract

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