The Experts below are selected from a list of 126 Experts worldwide ranked by ideXlab platform
Xiangmin Zhang - One of the best experts on this subject based on the ideXlab platform.
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Microchip reactor packed with metal-ion chelated magnetic silica microspheres for highly efficient proteolysis.
Journal of Proteome Research, 2007Co-Authors: Yan Li, Xiuqing Xu, Chunhui Deng, Pengyuan Yang, Wenjia Yu, Xiangmin ZhangAbstract:An easily replaceable and regenerable protease microreactor with metal-ion chelated Adsorption of Enzyme has been fabricated on chip. Magnetic microspheres with small size (∼200 nm in diameter) and strong magnetism were synthesized and were modified with tetraethyl orthosilicate. The metal chelating agent of iminodiacetic acid was then reacted with glycidoxypropyltrimethoxysilane before its immobilization onto the surface of magnetic silica microspheres (MS microspheres). The metal ion of copper and Enzyme were subsequently adsorbed onto the surface. The prepared MS microspheres were then locally packed into the microchannel by the application of a strong magnetic field using a magnet to form an on-chip enzymatic microreactor. Capability of the proteolytic microreactor was demonstrated by cytochrome c and bovine serum albumin as model proteins. The digestion products were characterized using MALDI-Tof/Tof MS with sequence coverage of 77% and 21% observed, respectively. This microreactor was also applied t...
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On-column tryptic mapping of proteins using metal-ion-chelated magnetic silica microspheres by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
Rapid Communications in Mass Spectrometry, 2007Co-Authors: Yan Li, Xiuqing Xu, Bo Yan, Chunhui Deng, Xizhong Shen, Pengyuan Yang, Xiangmin ZhangAbstract:Peptide mapping analysis, utilizing an easily replaceable and regenerable on-column enzymatic microreactor with metal-ion-chelated Adsorption of Enzyme on magnetic silica microspheres, combined with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDITof MS), was developed. Firstly, magnetic microspheres of small size and strong magnetism were prepared through solvothermal reaction. Thereafter, by introducing tetraethyl orthosilicate (TEOS), magnetic silica (MS) microspheres were formed. Trypsin could then be immobilized onto the MS microspheres based on the Lewis acid-base interaction through the divalent cation chelators such as iminodiacetic acid (IDA), which was chemically bound to the microspheres through the introduction of glycidoxypropyltrimethoxysilane (GLYMO). The trypsin-immobilized MS microspheres were then locally packed into the capillary by the application of a strong magnetic field using a magnet. The performance of the method was exemplified with digestion of bovine serum albumin for 5 min at 50 degrees C and the result was comparable to the 12 h in-solution digestion. The ability of regeneration of the prepared on-column microreactor and good reproducibility of microreactor before and after regeneration were also demonstrated. Copyright (C) 2007 John Wiley & Sons, Ltd.
Baochuan Guo - One of the best experts on this subject based on the ideXlab platform.
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Immobilized metal-ion chelating capillary microreactor for peptide mapping analysis of proteins by matrix assisted laser desorption/ionization-time of flight-mass spectrometry
Electrophoresis, 2003Co-Authors: Zhong Guo, Zhengdeng Lei, Hanfa Zou, Songyun Xu, Baochuan GuoAbstract:Peptide mass mapping analysis, utilizing a regenerable Enzyme microreactor with metal-ion chelated Adsorption of Enzyme, combined with matrix assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-Tof-MS) was developed. Different procedures from the conventional approaches were adopted to immobilize the chelator onto the silica supports, that is, the metal chelating agent of iminodiacetic acid (IDA) was reacted with glycidoxypropyltrimethoxysilane (GLYMO) before its immobilization onto the inner wall of the fused-silica capillary pretreated with NH4HF2. The metal ion of copper and subsequently Enzyme was specifically adsorbed onto the surface to form the immobilized Enzyme capillary microreactor, which was combined with MALDI-Tof-MS to apply for the mass mapping analysis of nL amounts of protein samples. The results revealed that the peptide mapping could routinely be generated from 0.5 pmol protein sample in 15 min at 50degreesC, even 20 fmol cytochrome c could be well digested and detected.
Yan Li - One of the best experts on this subject based on the ideXlab platform.
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Microchip reactor packed with metal-ion chelated magnetic silica microspheres for highly efficient proteolysis.
Journal of Proteome Research, 2007Co-Authors: Yan Li, Xiuqing Xu, Chunhui Deng, Pengyuan Yang, Wenjia Yu, Xiangmin ZhangAbstract:An easily replaceable and regenerable protease microreactor with metal-ion chelated Adsorption of Enzyme has been fabricated on chip. Magnetic microspheres with small size (∼200 nm in diameter) and strong magnetism were synthesized and were modified with tetraethyl orthosilicate. The metal chelating agent of iminodiacetic acid was then reacted with glycidoxypropyltrimethoxysilane before its immobilization onto the surface of magnetic silica microspheres (MS microspheres). The metal ion of copper and Enzyme were subsequently adsorbed onto the surface. The prepared MS microspheres were then locally packed into the microchannel by the application of a strong magnetic field using a magnet to form an on-chip enzymatic microreactor. Capability of the proteolytic microreactor was demonstrated by cytochrome c and bovine serum albumin as model proteins. The digestion products were characterized using MALDI-Tof/Tof MS with sequence coverage of 77% and 21% observed, respectively. This microreactor was also applied t...
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On-column tryptic mapping of proteins using metal-ion-chelated magnetic silica microspheres by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
Rapid Communications in Mass Spectrometry, 2007Co-Authors: Yan Li, Xiuqing Xu, Bo Yan, Chunhui Deng, Xizhong Shen, Pengyuan Yang, Xiangmin ZhangAbstract:Peptide mapping analysis, utilizing an easily replaceable and regenerable on-column enzymatic microreactor with metal-ion-chelated Adsorption of Enzyme on magnetic silica microspheres, combined with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDITof MS), was developed. Firstly, magnetic microspheres of small size and strong magnetism were prepared through solvothermal reaction. Thereafter, by introducing tetraethyl orthosilicate (TEOS), magnetic silica (MS) microspheres were formed. Trypsin could then be immobilized onto the MS microspheres based on the Lewis acid-base interaction through the divalent cation chelators such as iminodiacetic acid (IDA), which was chemically bound to the microspheres through the introduction of glycidoxypropyltrimethoxysilane (GLYMO). The trypsin-immobilized MS microspheres were then locally packed into the capillary by the application of a strong magnetic field using a magnet. The performance of the method was exemplified with digestion of bovine serum albumin for 5 min at 50 degrees C and the result was comparable to the 12 h in-solution digestion. The ability of regeneration of the prepared on-column microreactor and good reproducibility of microreactor before and after regeneration were also demonstrated. Copyright (C) 2007 John Wiley & Sons, Ltd.
Zhong Guo - One of the best experts on this subject based on the ideXlab platform.
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Immobilized metal-ion chelating capillary microreactor for peptide mapping analysis of proteins by matrix assisted laser desorption/ionization-time of flight-mass spectrometry
Electrophoresis, 2003Co-Authors: Zhong Guo, Zhengdeng Lei, Hanfa Zou, Songyun Xu, Baochuan GuoAbstract:Peptide mass mapping analysis, utilizing a regenerable Enzyme microreactor with metal-ion chelated Adsorption of Enzyme, combined with matrix assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-Tof-MS) was developed. Different procedures from the conventional approaches were adopted to immobilize the chelator onto the silica supports, that is, the metal chelating agent of iminodiacetic acid (IDA) was reacted with glycidoxypropyltrimethoxysilane (GLYMO) before its immobilization onto the inner wall of the fused-silica capillary pretreated with NH4HF2. The metal ion of copper and subsequently Enzyme was specifically adsorbed onto the surface to form the immobilized Enzyme capillary microreactor, which was combined with MALDI-Tof-MS to apply for the mass mapping analysis of nL amounts of protein samples. The results revealed that the peptide mapping could routinely be generated from 0.5 pmol protein sample in 15 min at 50degreesC, even 20 fmol cytochrome c could be well digested and detected.
Pengyuan Yang - One of the best experts on this subject based on the ideXlab platform.
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Microchip reactor packed with metal-ion chelated magnetic silica microspheres for highly efficient proteolysis.
Journal of Proteome Research, 2007Co-Authors: Yan Li, Xiuqing Xu, Chunhui Deng, Pengyuan Yang, Wenjia Yu, Xiangmin ZhangAbstract:An easily replaceable and regenerable protease microreactor with metal-ion chelated Adsorption of Enzyme has been fabricated on chip. Magnetic microspheres with small size (∼200 nm in diameter) and strong magnetism were synthesized and were modified with tetraethyl orthosilicate. The metal chelating agent of iminodiacetic acid was then reacted with glycidoxypropyltrimethoxysilane before its immobilization onto the surface of magnetic silica microspheres (MS microspheres). The metal ion of copper and Enzyme were subsequently adsorbed onto the surface. The prepared MS microspheres were then locally packed into the microchannel by the application of a strong magnetic field using a magnet to form an on-chip enzymatic microreactor. Capability of the proteolytic microreactor was demonstrated by cytochrome c and bovine serum albumin as model proteins. The digestion products were characterized using MALDI-Tof/Tof MS with sequence coverage of 77% and 21% observed, respectively. This microreactor was also applied t...
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On-column tryptic mapping of proteins using metal-ion-chelated magnetic silica microspheres by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
Rapid Communications in Mass Spectrometry, 2007Co-Authors: Yan Li, Xiuqing Xu, Bo Yan, Chunhui Deng, Xizhong Shen, Pengyuan Yang, Xiangmin ZhangAbstract:Peptide mapping analysis, utilizing an easily replaceable and regenerable on-column enzymatic microreactor with metal-ion-chelated Adsorption of Enzyme on magnetic silica microspheres, combined with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDITof MS), was developed. Firstly, magnetic microspheres of small size and strong magnetism were prepared through solvothermal reaction. Thereafter, by introducing tetraethyl orthosilicate (TEOS), magnetic silica (MS) microspheres were formed. Trypsin could then be immobilized onto the MS microspheres based on the Lewis acid-base interaction through the divalent cation chelators such as iminodiacetic acid (IDA), which was chemically bound to the microspheres through the introduction of glycidoxypropyltrimethoxysilane (GLYMO). The trypsin-immobilized MS microspheres were then locally packed into the capillary by the application of a strong magnetic field using a magnet. The performance of the method was exemplified with digestion of bovine serum albumin for 5 min at 50 degrees C and the result was comparable to the 12 h in-solution digestion. The ability of regeneration of the prepared on-column microreactor and good reproducibility of microreactor before and after regeneration were also demonstrated. Copyright (C) 2007 John Wiley & Sons, Ltd.
